Title of Invention: Methods for Modulating Angiogenesis of Cancers Refractory to Anti-VEGF Treatment Abstract: A method for modulating angiogenesis in a cancer or tumor refractory to anti-VEGF, including identifying a cancer cell as being referactory to anti-VEGF, and then contacting the cancer cell refractory to anti-VEGF with an effective amount of an agent that modulates interaction between Gal1 or a Gal1 fragment and the natural binding partner of Gal1 or the Gal1 fragment to thereby modulate angiogenesis. Detailed Description: CROSS-REFERENCE TO RELATED APPLICATION This application claims the benefit of U.S. Provisional Application No. 61/909,942, filed on Nov. 27, 2013. The contents of the provisional application are hereby incorporated by reference herein. BACKGROUND Genetic and pharmacological disruption of vascular signaling pathways have provided unequivocal evidence that abnormal angiogenesis is a hallmark feature of cancer (Hanahan and Weinberg (2011); Chung and Ferrara, Annu. Rev. Cell Dev. Biol. 27, 563-584 (2011); Carmeliet and Jain, Nature 473, 298-307 (2011)). Cancer cells adapt to low oxygen tension by promoting the expression of genes associated with anaerobic metabolism, invasion and angiogenesis (Pugh et al., Nat. Med. 9, 677-684 (2003); Fraisl et al., Dev. Cell 16, 167-179 (2009)). The concerted action of hypoxia-regulated pathways allows tumor cells to sprout new vessels, co-opt host vessels and/or recruit angio-competent bone marrow-derived cells to generate functionally abnormal tumor vasculatures (Ferrara et al., Nature 438, 967-974 (2005)). Vascular endothelial growth factors (VEGFs) play central roles in this process through activation of VEGF receptor tyrosine kinases (RTKs), including VEGFR1 (Flt-1), VEGFR2 (KDR/Flk-1) and VEGFR3 (Flt-4), on endothelial cells (ECs) (Chung and Ferrara, Annu. Rev. Cell Dev. Biol. 27, 563-584 (2011)). Blockade of VEGF-A signaling with BEVACIZUMAB, a humanized anti-VEGF monoclonal antibody (mAb) or with RTK inhibitors, such as SUNITINIB or SORAFENIB, has improved progression-free survival for patients with several types of cancers, including metastatic colorectal cancer, advanced non-small cell lung cancer, metastatic breast cancer, renal cell carcinoma and advanced hepatocarcinoma (Kerbel (2008); Ellis and Hicklin, Nat. Rev. Cancer, 8:8, 579-91 (2008)). However, although approved therapies targeting VEGF-A have offered considerable clinical benefit, many patients whose tumors initially responded eventually become non-responsive, suggesting the contribution of compensatory pathways that preserve angiogenesis in VEGF-targeted therapies (Bergers and Hanahan, Nat. Rev. Cancer 8:8, 592-603 (2008)). For tumors having evasive resistance or intrinsic refractoriness (“tumors refractory to anti-VEGF” or “anti-VEGF refractory tumors” herein), the approved therapies targeting VEGF-A fail to produce enduring clinical benefits. There remains a need in the art for treating or inhibiting tumors that are refractory to conventional anti-VEGF treatments. SUMMARY Provided are methods for modulating angiogenesis in a cancer (or tumor) refractory to anti-VEGF treatment. In embodiments, methods for modulating angiogenesis in a refractory cancer (or tumor) may include identifying a cancer cell as being refractory to anti-VEGF, and then contacting (in vivo or in vitro) the refractory cancer cell with an effective amount of an agent that modulates interaction between Gal1 or a Gal1 fragment and a natural binding partner of Gal1 or the Gal1 fragment to thereby modulate angiogenesis. The modulating of angiogenesis preferably results in inhibition of angiogenesis in the refractory cancer cell. The agent that modulates interaction between Gal1 or the Gal1 fragment and the natural binding partner of Gal1 or the Gal1 fragment inhibits may be, e.g., an antibody, a nucleic acid, a peptide, a fusion protein, a small molecule, or a glycan-related compound. In some embodiments, the agent that modulates interaction between Gal1 or the Gal1 fragment and the natural binding partner of Gal1 or the Gal1 fragment may be selected from the group consisting of: a blocking antibody or an antigen-binding fragment thereof that recognizes Gal1 or the Gal1 fragment; and a blocking antibody or an antigen-binding fragment thereof that recognizes the Gal1 or the Gal1 fragment natural binding partner. In certain embodiments, the agent that modulates interaction between Gal1 or the Gal1 fragment and the natural binding partner of Gal1 or the Gal1 fragment may be an anti-Gal1 monoclonal antibody or an antigen-binding fragment thereof. In still further embodiments, a monoclonal antibody that is selective for Gal1 over other galectins, or a fragment thereof, may be selected as as the agent that modulates interaction between Gal1 or the Gal1 fragment and the natural binding partner of Gal1 or the Gal1 fragment. Cancers (or tumors) in which angiogenesis may be modulated according to methods described herein may be refractory to anti-VEGF, such as LLCI Lewis lung carcinoma, R1.1 T cell lymphoma, and pancreatic cancer. Methods of modulating angiogenesis in a cancer (or tumor) refractory to anti-VEGF treatment may include, in addition to identifying a cancer cell as being refractory to anti-VEGF and then contacting the refractory cancer cell with an effective amount of an agent that modulates interaction between Gal1 or a Gal1 fragment and a natural binding partner of Gal1 or the Gal1 fragment, contacting the refractory cancer cell with one or more second agent that may include a blocking antibody or an antigen binding fragment thereof that recognizes Gal1, and/or a blocking antibody or an antigen binding fragment thereof that recognizes a Gal1 binding partner or a fragment thereof. In certain embodiments, the second agent may be that is an anti-angiogenic agent, such as, e.g., an anti-VEGF antibody. Provided herein are methods for treating a subject having a cancer (or tumor) refractory to anti-VEGF treatment, such methods including administering to the subject having the refractory cancer (or tumor) a therapeutically effective amount of an agent that inhibits interaction between Gal1 or a Gal1 fragment and the natural binding partner of Gal1 or the Gal1 fragment (i.e., a “modulating agent” as defined herein). The modulating agent administered to the subject is preferably therapeutically effective in: (a) slowing or inhibiting growth of the refractory cancer (or tumor); (b) preventing spreading of the refractory cancer (or tumor); (c) preventing recurrence of a previously spread tumor associated with the refractory cancer; (d) preventing spreading of one or more metastases associated with the refractory cancer (or tumor); (e) reducing the size of a tumor associated with the refractory cancer; and/or (f) preventing recurrence of the refractory cancer (or tumor) that has been previously treated. Methods for treating a subject having a cancer (or tumor) refractory to anti-VEGF treatment may include administering at least a second agent, wherein the second agent may include a blocking antibody or an antigen binding fragment thereof that recognizes Gal1, and/or a blocking antibody or an antigen binding fragment thereof that recognizes a Gal1 binding partner or a fragment thereof. The additional agent(s) may include one or more anti-VEGF antibody. In certain embodiments of the treatment methods described herein, the agent that inhibits interaction between Gal1 or the Gal1 fragment and the natural binding partner of Gal1 or the Gal1 fragment may be administered to a subject in a pharmaceutical composition that also comprises a pharmaceutically acceptable carrier selected from the group consisting of solvents, dispersion media, coatings, antibacterial agents, antifungal agents, isotonic agents and absorption delaying agents. The pharmaceutical composition may comprise: (a) as the active ingredient—an agent that inhibits interaction between Gal1 or the Gal1 fragment and the natural binding partner of Gal1 or the Gal1 fragment; and (b) as the carrier a pharmaceutical excipient selected from the group consisting of starch, glucose, lactose, sucrose, gelatin, malt, rice, flour, chalk, silica gel, sodium stearate, glycerol monostearate, talc, sodium chloride, dried skim milk, glycerol, propylene, glycol, water, and ethanol. Modes of administration of the active ingredient (modulating agent) according to methods provided herein include, but are not limited to, parenteral administration, intradermal administration, subcutaneous administration, oral administration, inhalation, transdermal administration, transmucosal administration, and rectal administration. In certain embodiments, the agent that inhibits interaction between Gal1 or a fragment thereof and a natural binding partner of Gal1 or the Gal1 fragment may be administered to a subject having a cancer (or tumor) refractory to anti-VEGF treatment in the form of, e.g., an injectable solution, an aerosol, a nasal spray, a suppository, a cream, a gel, a tablet, and a capsule. The agent may be a nucleic acid that has been inserted into a vector, and the vector administered to the subject in need thereof in a composition by intravenous injection, local injection, or sterotactic injection. Prophylactic methods for preventing angiogenesis in cancers (or tumors) refractory to anti-VEGF treatment may comprise administering to a subject susceptible or at risk for having a cancer refractory to anti-VEGF treatment an effective amount of an agent that binds to the Gal1 gene or a fragment thereof to attenuate hypoxia-associated angiogenesis. In embodiments, the agent that binds to the Gal1 gene or a fragment thereof may be an anti-Gal1 antibody, and may be administered to the subject susceptible or at risk for having a cancer refractory to anti-VEGF treatment in a vaccine composition. In some embodiments, methods for treating a subject having a cancer (or tumor) refractory to anti-VEGF treatment comprise administering to the subject a therapeutically effective amount of an agent that inhibits the interaction between Gal1 or a fragment thereof and its natural binding partner(s). In some embodiments, methods for treating a subject having a cancer (or tumor) refractory to anti-VEGF treatment comprise administering to the subject a therapeutically effective amount of a pharmaceutical composition comprising an anti-Gal1 antibody and an anti-VEGF antibody. BRIEF DESCRIPTION OF THE DRAWINGS FIGS. 1A-1J show differential glycosylation of endothelial cells (ECs) controlling the formation of lectin-glycan lattices. FIG. 1A shows a schematic representation of N- and O-glycan biosynthesis, including relevant glycosyltransferases, such as α2-6 sialyltransferase 1 (ST6GAL1), N-acetylglucosaminyltransferase 5 (MOATS), α2-3 sialyltransferase 1 (ST3GAL1) and core 2 N-acetylglucosaminyltransferase 1 (C2GNT1). Coordinated actions of these glycosyltransferases lead to the generation or masking of common glycosylated ligands for galectins (N-acetyl lactosamine; LacNAc) or poly-LacNAc residues in complex N-glycans or core 2 O-glycans). FIG. 1A also shows a schematic representation of lectin-binding sites in N- and O-glycans. Specific residues recognized by MAL II, LEL, SNA and L-PHA on complex N-glycans and by HPA, PNA and LEL on O-glycans are indicated (green grayscales). The common glycosylated ligand for Gal1 (LacNAc) is also indicated (purple grayscales). FIG. 1B shows the glycan repertoire of HUVEC under resting conditions (2% FCS) detected with biotinylated L-PHA, LEL, SNA, MAL II, PNA and HPA (filled histograms) or with PE-conjugated stravidin alone (open histograms). Data are representative of eight experiments. FIG. 1C shows the glycan repertoire of HUVEC under resting, proliferative (bFGF), activated (VEGF-A), tolerogenic (IL-10 and/or TGF-β1) or pro-inflammatory (IFN-γ and/or IL-17) conditions. rMFI (relative mean fluorescence intensity)=(MFI with lectin−MFI without lectin)/MFI without lectin. Data are presented as the ratio relative to resting conditions (dotted line; value=1) and are the mean±SEM of four experiments. * P<0.05, ** P<0.01 versus resting. FIG. 1D shows binding results of 488-Gal1 to HUVEC with or without lactose or sucrose, swainsonine or benzyl-α-GalNAc. ** P<0.01. Data are the mean±SEM of four experiments. FIG. 1E shows binding results of 488-Gal1 to HUVEC transfected with MGAT5 or C2GNT1 siRNA. Cells without siRNA or transfected with scrambled (src) siRNA were used as controls. ** P<0.01. Data are the mean±SEM of four experiments. FIG. 1F shows binding results of 488-Gal1 to HUVEC exposed to tolerogenic, proliferative or inflammatory stimuli. Data are presented as the rMFI ratio relative to resting ECs (dotted line; value=1) and are the mean±SEM of four experiments. * P<0.05, ** P<0.01 versus resting. FIG. 1G shows the glycan repertoire on HUVEC incubated in hypoxia (black-filled greyscales histograms) or normoxia (grey-filled greyscales histograms), detected with biotinylated L-PHA, LEL, SNA, MAL II or PNA, or with PE-conjugated stravidin alone (open histograms). Data are representative of five experiments. FIG. 1H shows the results of glycan nanoprofiling of ECs exposed to normoxia or hypoxia. Bars represent the relative abundance of neutral, mono-, di-, tri-, and tetra-sialylated N-glycans from total N-glycans. * P<0.05. Data are the mean±SEM of three experiments. FIG. 1I shows the binding of 488-Gal1 to HUVEC exposed to hypoxia or normoxia. ** P<0.01. Data are the mean±SEM of five experiments. FIG. 1J shows tube formation of HUVEC transfected or not with MGAT5, C2GNT1 or scr siRNA and incubated with Gal1 (1 μM), Gal1N46D (3 μM) and/or VEGF-A (20 ng/ml) in the absence or presence of lactose or swainsonine. ** P<0.01 versus control, † P<0.05 versus Gal1. Data are the mean±SEM of five experiments. FIGS. 2A-2J show the galectin-1 co-opts VEGFR2 signaling pathways through the formation of lectin-glycan lattices on highly branched complex N-glycans. FIG. 2A shows results of a phospho-RTK signaling array of HUVEC exposed to medium (control), VEGF or Gal1, wherein in the left panel, arrows indicate proteins with increased phosphorylation intensity. Data are representative of three independent experiments. By contrast, the right panel shows quantification of pixel intensity. * P<0.05, ** P<0.01 versus control. Data are the mean±SEM of three independent experiments. FIG. 2B shows immunoblot analysis of VEGFR2, Akt and Erk1/2 phosphorylation induced by Gal1 or VEGF in HUVEC transfected with VEGFR2 or MGAT5 siRNA. Data are representative of three independent experiments. FIG. 2C shows tube formation results of HUVEC transfected or not with VEGFR2, NRP-1, VEGF or scr siRNA treated or not with Gal1. ** P<0.01. Data are the mean±SEM of four experiments. FIG. 2D shows tube formation results of HUVEC pre-treated with blocking antibodies to VEGFR1, VEGFR2, VEGFR3, integrins αvβ3 or α5β1 or VEGF. *** P<0.001. Data are the mean±SEM of four experiments. FIG. 2E shows co-immunoprecipitation results followed by immunoblot analysis of HUVEC lysates, wherein the left panel shows results from cells treated with or without Gal1 and the right panel shows results from cells transfected or not with MGAT5 or C2GNT1 siRNA or exposed to PNGase F and treated with Gal1. Input, whole cell lysate; IB, immunoblot; IP, immunoprecipitation. Data are representative of three independent experiments. FIG. 2F shows results of binding of Gal1 to rhVEGFR2 followed by FRET analysis. Left, fluorescence intensity at 518 nm measured at increasing concentrations of 594-Gal1. Right, fluorescence intensity at 518 nm of 0.5 μM 488-VEGFR2 in the presence of 594-Gal1 titrated with increasing concentrations of lactose. Data are representative of three experiments. FIG. 2G shows results of lectin blot analysis, showing selective sialylation of different VEGFRs, demonstrating the fine regulation of this process. FIG. 2H shows results of Gal1 binding to VEGFR2/KDR mutants devoid of N-glycosylation sites in each of the 7 Ig-like domains. Binding of Gal1 to immunoprecipitated KDR-HA mutants expressed as percentage relative to WT-KDR. * P<0.05, ** P<0.01 versus WT-KDR. Data are the mean±SEM of four independent experiments. FIG. 2I shows laser confocal microscopy results of VEGFR2 segregation in HUVEC transfected or not with MGAT5 or C2GNT1 siRNA and treated or not with Gal1 or Gal1 plus lactose. ** P<0.01, *** P<0.001. Data are the mean±SEM (left) or are representative (right) of four independent experiments. FIGS. 3A-3F show the relationship between differential EC glycosylation and refractoriness to anti-VEGF therapy. FIG. 3A shows tumor growth in syngeneic mice inoculated with B16-F0, CT26, LLC1 or R1.1 tumors treated with anti-VEGF mAb (5 mg/kg) or isotype control. * P<0.05. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 3B shows the percentage of tumor-associated ECs for the same mice. * P<0.05, ** P<0.01. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 3C shows the glycophenotype of ECs exposed to serum-free conditioned media collected from LLC1, R1.1, B16-F0 or CT26 tumor cells previously cultured in normoxia or hypoxia. * P<0.05, ** P<0.01, *** P<0.001. Data are the mean±SEM of four experiments. FIG. 3D shows the glycophenotype of ECs associated to LLC1 tumors in response to anti-VEGF treatment. * P<0.05, ** P<0.01. Data are the mean±SEM of four independent experiments. FIG. 3E shows the glycophenotype of ECs associated to B16-F0 tumors in response to anti-VEGF treatment. * P<0.05, ** P<0.01. Data are the mean±SEM of four independent experiments. FIG. 3F shows ELISA results of Gal1 secretion by LLC1, R1.1 or B16-F0 tumors in response to anti-VEGF treatment. * P<0.05. ** P<0.01. Data are the mean±SEM of four experiments. FIGS. 4A-4E show that tumors devoid of Gal1 circumvent refractoriness to anti-VEGF therapy. FIG. 4A shows tumor growth in syngeneic B6 mice inoculated with LLC1 or R1.1 tumors transduced with Gal1-specific shRNA (shGal1.1) or sh-scr and treated with anti-VEGF mAb. * P<0.05, ** P<0.01. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 4B shows the percentage of tumor-associated ECs in the same mice. ** P<0.01. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 4C shows tumor growth in Lgals1−/− B6 mice inoculated with LLC1 tumors transduced with shGal1.1 or sh-scr and treated with anti-VEGF mAb. ** P<0.01 versus sh-scr. Data are the mean±SEM of three independent experiments with six animals per group. FIG. 4D shows tumor growth in syngeneic B6 mice inoculated with B16-F0 tumors transduced with shGal1.1 or sh-scr and treated with anti-VEGF mAb. ** P<0.01. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 4E shows the percentage of tumor-associated in the same mice. ** P<0.01. Data are the mean±SEM of four independent experiments with six animals per group. FIGS. 5A-5G show that reprogramming of EC glycosylation converts anti-VEGF refractory tumors to sensitive tumors. FIG. 5A shows flow cytometry results of L-PHA staining in ECs associated to LLC1 tumors inoculated into WT or Mgat5−/− mice (day 16). Data are representative of four independent experiments with six animals per group. FIG. 5B shows tumor growth in Mgat5−/− or WT mice inoculated with LLC1 tumors and treated with anti-VEGF mAb (5 mg/kg) or isotype control. ** P<0.01 versus WT. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 5C shows the percentage of tumor-associated ECs in Mgat5−/− or WT mice inoculated with LLC1 tumors and treated with anti-VEGF mAb (5 mg/kg) or isotype control. *** P<0.001 versus WT. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 5D shows flow cytometry results of SNA staining in ECs associated with B16-F0 tumors inoculated into WT or St6gal1−/− mice (day 16). Data are representative of four independent experiments with six animals per group. FIG. 5E shows tumor growth in St6gal1−/− or WT mice inoculated with B16-F0 tumors and treated with anti-VEGF mAb (5 mg/kg) or isotype control. ** P<0.01 versus WT. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 5F shows the percentage of tumor-associated ECs in the same mice. *** P<0.001 versus WT. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 5G shows tumor growth in St6gal1−/− mice inoculated with B16-F0 tumors and treated with anti-VEGF mAb (5 mg/kg) or anti-VEGF mAb plus axitinib (30 mg/kg) or inoculated with B16-F0 tumors transduced with Gal1-specific shRNA (shGal1.1) and treated with anti-VEGF mAb. ** P<0.01. Data are the mean±SEM of three independent experiments with six animals per group. FIGS. 6A-6L show that targeting the Gal1-N-glycan axis promotes vascular remodeling and overcomes refractoriness to anti-VEGF therapy. FIG. 6A shows tube formation results of HUVEC induced by Gal1 or VEGF-A in the absence or presence of the anti-Gal1 (F8.G7) mAb or isotype control. ** P<0.01. Data are the mean±SEM of four experiments. FIG. 6B shows an immunoblot of VEGFR2 phosphorylation in HUVEC treated with Gal1 in the absence or presence of F8.G7 mAb or isotype control or in HUVEC transfected with MGAT5 siRNA. Results are representative of three independent experiments. FIG. 6C shows growth of LLC1 and microvessel density of tumors inoculated in syngeneic mice treated with anti-VEGF mAb or F8.G7 mAb (alone or in combination) or with isotype control. ** P<0.01. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 6D shows growth of R1.1. * P<0.05, ** P<0.01. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 6E shows growth of B16-F0 and microvessel density of tumors inoculated in syngeneic mice treated with anti-VEGF mAb or F8.G7 mAb (alone or in combination) or with isotype control. * P<0.05, ** P<0.01, *** P<0.001. Data are the mean±SEM of four independent experiments with six animals per group. FIG. 6F shows ELISA results of Gal1 secretion by B16-F0, LLC1 and R1.1 tumors (at day 16) inoculated in syngeneic mice and treated with anti-Gal1 F8.G7 mAb or isotype control. *** P<0.001. Data are the mean±SEM of four independent experiments with five animals per group. FIG. 6G shows confocal microscopy results of lectin (GLS-1B4)-perfused vessels in size-matched B16-F0 tumors inoculated in syngeneic mice and treated for 4-5 days with F8.G7 mAb or isotype control. The right panel quantifies vessel diameters. * P<0.05. Data are the mean±SEM of four independent experiments with six mice per group. FIG. 6H shows confocal microscopy results of lectin-perfused vessels (green grayscales) labeled with anti-α-SMA Ab (red grayscales) in sized-matched B16-F0 tumors inoculated in syngeneic mice and treated for 4-5 days with F8.G7 mAb or with isotype control. The right panel shows the percentage of tumor vessels showing pericyte coverage. ** P<0.01. Data are the mean±SEM of four independent experiments with six mice per group. FIG. 6I shows confocal microscopy results of RGS5, desmin, α-SMA and PDGFR-β in pericytes associated to vessels of B16-F0 tumors inoculated into syngeneic mice and treated for 4-5 days with F8.G7 mAb or isotype control. Quantification (left) and representative images (right) are shown. * P<0.05, ** P<0.01. Data are the mean±SEM of four independent experiments with six mice per group. FIG. 6J shows confocal microscopy of B16-F0 size-matched tumors stained with Hypoxiprobe-1. Data are the mean±SEM of four independent experiments with six mice per group. FIGS. 6K and 6L show confocal microscopy results of CD31 (FIG. 6K) and lectin-perfused vessels (green greyscales) labeled with anti-α-SMA Ab (red greyscales) (FIG. 6L) in LLC1 tumors inoculated into WT mice and treated with anti-Gal1 F8.G7 mAb or with isotype control or LLC1 tumors inoculated into Mgat5−/− mice. The right panel of FIG. 6K quantifies vessel diameter, and the right panel of FIG. 6L quantifies pericyte coverage. ** P<0.01. Data are the mean±SEM of four independent experiments with six mice per group. FIGS. 7A-7R show disruption of Gal1-N-glycan interactions controlling both vascular and immune compartments. FIGS. 7A-7D show proliferation results (FIG. 7A) and ELISA results of IFN-γ (FIG. 7B), IL-17 (FIG. 7C) and IL-10 (FIG. 7D) by TDLN cells from mice inoculated with B16-F0 tumor cells and treated with F8.G7 mAb or isotype control and restimulated ex vivo with B16 cells. ** P<0.01. Data are the mean±SEM of four independent experiments with six mice per group. FIGS. 7E-7G show ELISA results of IFN-γ (FIG. 7E), IL-17 (FIG. 7F) and IL-10 (FIG. 7G) secretion of IFN-γ-producing CD8+ T cells in TDLNs from mice inoculated with LLC1 cells and treated with F8.G7 mAb or isotype control. * P<0.05, *** P<0.001. Data are the mean±SEM of four independent experiments with six mice per group. FIG. 7H shows flow cytometry results of IFN-γ-producing CD8+ T cells in TDLNs from mice inoculated with B16-F0 cells and treated with F8.G7 mAb or isotype control. ** P<0.01. Data are the mean±SEM of four independent experiments with six mice per group. FIG. 7I shows flow cytometry results of IFN-γ-producing CD8+ T cells in TDLNs from mice inoculated with LLC1 cells and treated with F8.G7 mAb or isotype control. ** P<0.01. Data are the mean±SEM of four independent experiments with six mice per group. FIG. 7J shows confocal microscopy results of tumor-infiltrating CD8+ T cells in mice inoculated with B16-F0 tumor cells and treated with F8.G7 mAb or isotype control. ** P<0.01. Data in the left panel are representative of four independent experiments with six mice per group; data in the right panel are the mean±SEM of four independent experiments with six mice per group. FIGS. 7K-7O show ELISA results of IFN-γ (FIG. 7K), IL-17 (FIG. 7L) and IL-10 (FIG. 7M) and flow cytometry results of IFN-γ-producing CD4+ (FIG. 7N) or CD8+ (FIG. 7O) T cells in TDLNs from Mgat5−/− mice inoculated with LLC1 tumors. * P<0.05, ** P<0.01, *** P<0.001. Data are the mean±SEM (FIGS. 7L-7N) or are representative (FIG. 7O) of four independent experiments with six mice per group. FIGS. 7P and 7Q show confocal microscopy results of tumor-infiltrating CD8+ T cells (FIG. 7P) and F4/80+ macrophages (FIG. 7Q) in Mgat5−/− or WT mice inoculated with LLC1 tumors. * P<0.05. Data in the left panel of FIG. 7P are representative of four independent experiments with six mice per group. Data in the right panel of FIG. 7P and in FIG. 7Q are the mean±SEM of four independent experiments with six mice per group. FIG. 7R shows flow cytometry analysis of T cell influx to tumor parenchyma or spleen. Spleen T cells were purified from tumor (B16-F0)-bearing mice, stained with CFSE and transferred (5×106) to mice with established tumors treated with F8.G7 mAb or isotype control. Data are representative of four independent experiments with six mice per group. FIGS. 8A-8C show that differential EC glycosylation defines tumor refractoriness to anti-VEGF therapy. FIG. 8B shows ELISA results of bFGF (left), TGF-β1 (middle) and VEGF-A (right) secretion by LLC1, R1.1, B16-F0 and CT26 tumor cells exposed to normoxia or hypoxia. * P<0.05, ** P<0.01, *** P<0.001. Data are the mean±SEM of two independent experiments. FIG. 8C shows ELISA results of Gal3 or Gal8 secretion by refractory (LLC1, R1.1) or sensitive (B16-F0) tumors in response to anti-VEGF treatment. Data are the mean±SEM of three independent experiments. FIGS. 9A-9D show tumors devoid of Gal1 circumventing refractoriness to anti-VEGF therapy. FIG. 9A shows an immunoblot of Gal1 in total lysates of LLC1, R1.1 and B16-F0 non-transduced tumor cells (WT) or transduced with two different Gal1-specific shRNA (shGal1.1, shGal1.2) or with scrambled shRNA (sh-scr). Data are representative of three independent experiments. FIG. 9B shows the results of an MTS proliferation assay of LLC1, R1.1 and B16-F0 non-transduced tumor cells (WT) or tumor cells transduced with shGal1.1 or control sh-scr. Data are the mean±SEM of four experiments. FIG. 9C shows that tumor growth results in syngeneic B6 mice inoculated with B16-F0 tumors transduced with shGal1.1 (bulk) or a clone obtained by limiting dilution (shGal1.1-c) or control sh-scr. * P<0.05 versus sh-scr. Data are the mean±SEM of four independent experiments with six mice per group. FIG. 9D shows the results of immunoblot analysis of Gal3, Gal4, Gal7 and Gal8 in lysates of B16-F0 cells transduced with shGal1.1 or sh-scr. Data are representative of two independent experiments. FIGS. 10A and 10B show that targeting the Gal1-N-glycan axis promotes vascular remodeling and overcomes refractoriness to anti-VEGF therapy. FIG. 10A shows migration of HUVEC induced by Gal1 or VEGF-A in the absence or presence of the anti-Gal1 (F8.G7) mAb or isotype control. ** P<0.01. Data are representative (left) or are the mean±SEM of four independent experiments. FIG. 10B shows the dose-dependent effect of anti-Gal1 (F8.G7) mAb. Tumor growth in syngeneic mice inoculated with B16-F0 tumors and treated with different doses of anti-Gal1 F8.G7 mAb or with isotype control when tumors reached 100 mm3. * P<0.05, ** P<0.01. Data are the mean±SEM of four independent experiments with six mice per group. FIGS. 11A-11C show that disruption of Gal1-N-glycan interactions controls both vascular and immune compartments. FIG. 11A shows tumor growth results in B6.Rag1−/− mice inoculated with B16-F0 tumors and treated with F8.G7 mAb or with isotype control when tumors reached 100 mm3. * P<0.05. Data are the mean±SEM of two independent experiments with six animals per group. FIG. 11B shows the number of fluorescently—labeled beads (relative to 1×106 events) reaching tumor and spleen of mice inoculated with B16-F0 tumors and treated with F8.G7 mAb or with isotype control. **P<0.01. Data are the mean±SEM of two independent experiments with four animals per group. FIG. 11C shows the number of fluorescently-labeled beads (relative to 1×106 events) reaching the tumor of Mgat5−/− or WT mice inoculated with LLC1 cells. ** P<0.01. Data are the mean±SEM of two independent experiments with four mice per group. FIG. 12 shows confocal microscopy data of anti-VEGF treated PDAC and anti-ragweed-treated PDAC. FIG. 13A is a schematic flowchart of anti-VEGF treatment for sensitive and refractory tumors that is based on the glycolysation-dependent pathway for modulating angiogenesis in response to the VEGF blockade described herein. As shown by the right-hand tumor, vessels within anti-VEGF sensitive tumors exhibit high levels of α2-6-linked sialic acid, which prevents Gal1 signaling and angiogenesis. However, as shown by the lower left-hand tumor, the vasculature of anti-VEGF refractory tumors expresses higher amounts of β1-6GlcNAc-branched N-glycans and decreased α2-6 sialylation due to an increase in secreted Gal1. As shown by the different tumors in FIG. 13A, interruption of β1-6GlcNAc-branching in ECs or silencing of tumor-derived Gal1 converts anti-VEGF refractory tumors into anti-VEGF sensitive tumors, whereas elimination of α2-6-linked sialic acid confers resistance to anti-VEGF. FIG. 13B is a schematic drawing showing how Gal1 mimics VEGF-A signaling through binding to complex N-glycans on VEGFR2 Ig domains (glycosylation sites) Ig-3, Ig-4, and Ig-7. DEFINITIONS When introducing elements of various embodiments, the articles “a,” “an,” “the” and “said” are intended to mean that there are one or more of the elements. The terms “comprising,” “including” and “having” are intended to be inclusive and mean that there may be additional elements other than the listed elements. Additional terms are defined below. The term “Gal1” as used herein refers to known Galectin-1 sequences, domains, fragments, and variants thereof, as well as gene products of the Gal1 gene and/or modulators thereof. The term “Gal1” also refers to a glycan-binding protein belonging to a highly-conserved family of animal lectins. Sequences, structures, domains, biophysical characteristics, and functions of Gal1 genes and gene products have been described in the art. See, e.g., Rabinovich et al., Trends Immunol. 23:313-320 (2002); Liu and Rabinovich, Nature Reviews Cancer 5:29-41 (2005); Rubinstein et al., Cancer Cell 5:241-251 (2004); Le et al., J. Clin. Oncol. 23:8932-8941 (2005); Vasta et al., Curr. Opin. Struct. Biol. 14:617-630 (2004); Toscano et al., Cyt. Growth Fact. Rev. 18:57-71 (2007); Camby et al., Glycobiology 16:137R-157R (2006) (the disclosures of the cited reference being incorporated by reference herein in their entireties). The Gal1 gene is also expressed in other cells known in the art. See, e.g., Gottschalk et al., Annu. Rev. Med. 56, 29-44 (2005); Nalesnik et al., Clin. Transplant. 13, 39-44 (1999); Toscano et al., Nat. Immunol. 8, 825-834 (2007); Ilarregui et al., Nat. Immunol. 10, 981-991 (2009); Re et al., J. Clin. Oncol. 23, 6379-6386 (2005); Marshall et al., Blood 103, 1755-1762 (2004); Gandhi et al., Blood 108, 2280-2289 (2006); Juszczynski et al., Proc. Natl. Acad. Sci. U.S.A. 104, 13134-13139 (2007); Rodig et al., Clin. Cancer Res. 14, 3338-3344 (2008); Rabinovich et al., Trends Immunol. 23:313-320 (2002); Liu and Rabinovich, Nature Reviews Cancer 5:29-41 (2005); Rubinstein et al., Cancer Cell 5:241-251 (2004); Le et al., J. Clin. Oncol. 23:8932-8941 (2005); Vasta et al., Curr. Opin. Struct. Biol. 14:617-630 (2004); Toscano et al., Cyt. Growth Fact. Rev. 18:57-71 (2007); Camby et al., Glycobiology 16:137 R-157R (2006). Human Gal1 sequences include those listed below. Gal1 Coding Nucleic Acid Sequence (SEQ ID NO: 1) ATGGCTTGTGGTCTGGTCGCCAGCAACCTGAATCTCAAACCTGGAGAGTG CCTTCGAGTGCGAGGCGAGGTGGCTCCTGACGCTAAGAGCTTCGTGCTGA ACCTGGGCAAAGACAGCAACAACCTGTGCCTGCACTTCAACCCTCGCTTC AACGCCCACGGCGACGCCAACACCATCGTGTGCAACAGCAAGGACGGCGG GGCCTGGGGGACCGAGCAGCGGGAGGCTGTCTTTCCCTTCCAGCCTGGAA GTGTTGCAGAGGTGTGCATCACCTTCGACCAGGCCAACCTGACCGTCAAG CTGCCAGATGGATACGAATTCAAGTTCCCCAACCGCCTCAACCTGGAGGC CATCAACTACATGGCAGCTGACGGTGACTTCAAGATCAAATGTGTGGCCT TTGACTGA Gal1 Protein Sequence (SEQ ID NO: 2) MACGLVASNLNLKPGECLRVRGEVAPDAKSFVLNLGKDSNNLCLHFNPRF NAHGDANTIVCNSKDGGAWGTEQREAVFPFQPGSVAEVCITFDQANLTVK LPDGYEFKFPNRLNLEAINYMAADGDFKIKCVAFD A “Gal1 antagonist” refers to a molecule (peptidyl or non-peptidyl) capable of neutralizing, blocking, inhibiting, abrogating, reducing or interfering with activities of a Gal1 sequence, including its binding to one or more Gal1 receptors. Gal1 antagonists include anti-Gal1 antibodies and antigen-binding fragments thereof, receptor molecules and derivatives that bind specifically to Gal1, thereby sequestering its binding to one or more receptors (e.g., soluble Gal1 receptor proteins or Gal1 binding fragments thereof, or chimeric Gal1 receptor proteins), anti-Gal1 receptor antibodies and Gal1 receptor antagonists, such as small molecule inhibitors of the Gal1 tyrosine kinases, and fusion proteins. Gal1 antagonists according to embodiments may include antagonists of Gal1, antisense molecules directed to Gal1, RNA aptamers, and ribozymes against Gal1 or Gal1 receptors. Gal1 antagonists useful in embodiments may further include peptidyl or non-peptidyl compounds that specifically bind Gal1, such as anti-Gal1 antibodies and antigen-binding fragments thereof, polypeptides, antibody variants or fragments thereof that specifically bind to Gal1, antisense nucleic oligomers complementary to at least a fragment of a nucleic acid molecule encoding a Gal1 polypeptide, small RNAs complementary to at least a fragment of a nucleic acid molecule encoding a VEGF polypeptide, ribozymes that target Gal1, peptibodies to Gal1, and Gal1 aptamers. In embodiments, the Gal1 antagonist reduces or inhibits, by at least 10%, or more, the expression level or biological activity of Gal1. The term “anti-Gal1 antibody” refers to an antibody that is capable of binding to Gal1 with sufficient affinity. In embodiments, the anti-Gal1 antibody may be used as a therapeutic agent in targeting and interfering with diseases or conditions in which Gal1 activity is involved. The antibody selected will normally have a sufficiently strong binding affinity for Gal1. Antibody affinities may be determined by a surface plasmon resonance based assay (such as the BIACORE assay described in PCT Application Publication No. WO 2005/012359), enzyme-linked immunoabsorbent assay (ELISA), and/or competition assays (e.g., RIAs). The terms “VEGF” and “VEGF-A” are used interchangeably to refer to the native sequence 165 amino acid vascular endothelial cell growth factor and related 121-, 145-, 183-, 189-, and 206-amino acid vascular endothelial cell growth factors together with the naturally occurring allelic and processed forms thereof, as well as variants thereof. See, e.g., Leung et al., Science, 246:1306 (1989); Houck et al., Mol. Endocrin., 5:1806 (1991); and Robinson & Stringer, Journal of Cell Science, 144(5):853-865 (2001)). VEGF-A is part of a gene family that includes VEGF-B, VEGF-C, VEGF-D, VEGF-E, VEGF-F, and PIGF. VEGFs primarily bind to VEGF receptor tyrosine kinases (RTKs), including VEGFR1 (Flt-1), VEGFR2 (Flk-1/KDR) and VEGFR3 (Flt-4) on endothelial cells (ECs) (see Chung and Ferrara, Annu. Rev. Cell Dev. Biol. 27, 563-584 (2011)). Sequences, structures, domains, biophysical characteristics, and functions of VEGFR2 genes and gene products, and glycosylated forms thereof, have been described in the art. See, e.g., Terman et al., Biochem. Biophys. Res. Commun. 187:1579-1586 (1992); Witte et al., Cancer Metastasis 17:155-161 (1998); Ortega et al., Front. Biosci. 4:D141-D152 (1999); Shibuya, Biol. Chem. 383:1573-1579 (2002); Olsson et al., Nat. Rev. Mol. Cell. Biol. 7:359-371 (2006); and Shibuya, J. Biochem. Mol. Biol. 39:469-478 (2006). Known VEGFR2 genes and gene products include those for, e.g., chimpanzee VEGFR2 (NCBI Accession XM_517284.2 and XP_517284.2), dog VEGFR2 (NCBI Accession XM_539273.2 and XP_539273.2), cow VEGFR2 (NCBI Accession XM_611785.3 and XP_611785.3), mouse VEGFR2 (NCBI Accession NM_010612.2 and NP_034742.2) and chicken Gal1 (NM_001004368.1 and NP_001004368.1). In addition, glycosylated forms of VEGFR2 are also known, as described by, e.g., Zhang et al., Cell Death Differ. 17:499 (2010) (incorporated by reference herein in its entirety). Accordingly, the terms “VEGF” or “VEGF-A” also refer to VEGFs from non-human species, such as, for example, mouse, rat or primate. Human VEGFR2 sequences include those provided below. VEGFR2 Coding Nucleic Acid Sequence (SEQ ID NO: 3) ATGCAGAGCAAGGTGCTGCTGGCCGTCGCCCTGTGGCTCTGCGTGGAGAC CCGGGCCGCCTCTGTGGGTTTGCCTAGTGTTTCTCTTGATCTGCCCAGGC TCAGCATACAAAAAGACATACTTACAATTAAGGCTAATACAACTCTTCAA ATTACTTGCAGGGGACAGAGGGACTTGGACTGGCTTTGGCCCAATAATCA GAGTGGCAGTGAGCAAAGGGTGGAGGTGACTGAGTGCAGCGATGGCCTCT TCTGTAAGACACTCACAATTCCAAAAGTGATCGGAAATGACACTGGAGCC TACAAGTGCTTCTACCGGGAAACTGACTTGGCCTCGGTCATTTATGTCTA TGTTCAAGATTACAGATCTCCATTTATTGCTTCTGTTAGTGACCAACATG GAGTCGTGTACATTACTGAGAACAAAAACAAAACTGTGGTGATTCCATGT CTCGGGTCCATTTCAAATCTCAACGTGTCACTTTGTGCAAGATACCCAGA AAAGAGATTTGTTCCTGATGGTAACAGAATTTCCTGGGACAGCAAGAAGG GCTTTACTATTCCCAGCTACATGATCAGCTATGCTGGCATGGTCTTCTGT GAAGCAAAAATTAATGATGAAAGTTACCAGTCTATTATGTACATAGTTGT CGTTGTAGGGTATAGGATTTATGATGTGGTTCTGAGTCCGTCTCATGGAA TTGAACTATCTGTTGGAGAAAAGCTTGTCTTAAATTGTACAGCAAGAACT GAACTAAATGTGGGGATTGACTTCAACTGGGAATACCCTTCTTCGAAGCA TCAGCATAAGAAACTTGTAAACCGAGACCTAAAAACCCAGTCTGGGAGTG AGATGAAGAAATTTTTGAGCACCTTAACTATAGATGGTGTAACCCGGAGT GACCAAGGATTGTACACCTGTGCAGCATCCAGTGGGCTGATGACCAAGAA GAACAGCACATTTGTCAGGGTCCATGAAAAACCTTTTGTTGCTTTTGGAA GTGGCATGGAATCTCTGGTGGAAGCCACGGTGGGGGAGCGTGTCAGAATC CCTGCGAAGTACCTTGGTTACCCACCCCCAGAAATAAAATGGTATAAAAA TGGAATACCCCTTGAGTCCAATCACACAATTAAAGCGGGGCATGTACTGA CGATTATGGAAGTGAGTGAAAGAGACACAGGAAATTACACTGTCATCCTT ACCAATCCCATTTCAAAGGAGAAGCAGAGCCATGTGGTCTCTCTGGTTGT GTATGTCCCACCCCAGATTGGTGAGAAATCTCTAATCTCTCCTGTGGATT CCTACCAGTACGGCACCACTCAAACGCTGACATGTACGGTCTATGCCATT CCTCCCCCGCATCACATCCACTGGTATTGGCAGTTGGAGGAAGAGTGCGC CAACGAGCCCAGCCAAGCTGTCTCAGTGACAAACCCATACCCTTGTGAAG AATGGAGAAGTGTGGAGGACTTCCAGGGAGGAAATAAAATTGAAGTTAAT AAAAATCAATTTGCTCTAATTGAAGGAAAAAACAAAACTGTAAGTACCCT TGTTATCCAAGCGGCAAATGTGTCAGCTTTGTACAAATGTGAAGCGGTCA ACAAAGTCGGGAGAGGAGAGAGGGTGATCTCCTTCCACGTGACCAGGGGT CCTGAAATTACTTTGCAACCTGACATGCAGCCCACTGAGCAGGAGAGCGT GTCTTTGTGGTGCACTGCAGACAGATCTACGTTTGAGAACCTCACATGGT ACAAGCTTGGCCCACAGCCTCTGCCAATCCATGTGGGAGAGTTGCCCACA CCTGTTTGCAAGAACTTGGATACTCTTTGGAAATTGAATGCCACCATGTT CTCTAATAGCACAAATGACATTTTGATCATGGAGCTTAAGAATGCATCCT TGCAGGACCAAGGAGACTATGTCTGCCTTGCTCAAGACAGGAAGACCAAG AAAAGACATTGCGTGGTCAGGCAGCTCACAGTCCTAGAGCGTGTGGCACC CACGATCACAGGAAACCTGGAGAATCAGACGACAAGTATTGGGGAAAGCA TCGAAGTCTCATGCACGGCATCTGGGAATCCCCCTCCACAGATCATGTGG TTTAAAGATAATGAGACCCTTGTAGAAGACTCAGGCATTGTATTGAAGGA TGGGAACCGGAACCTCACTATCCGCAGAGTGAGGAAGGAGGACGAAGGCC TCTACACCTGCCAGGCATGCAGTGTTCTTGGCTGTGCAAAAGTGGAGGCA TTTTTCATAATAGAAGGTGCCCAGGAAAAGACGAACTTGGAAATCATTAT TCTAGTAGGCACGGCGGTGATTGCCATGTTCTTCTGGCTACTTCTTGTCA TCATCCTACGGACCGTTAAGCGGGCCAATGGAGGGGAACTGAAGACAGGC TACTTGTCCATCGTCATGGATCCAGATGAACTCCCATTGGATGAACATTG TGAACGACTGCCTTATGATGCCAGCAAATGGGAATTCCCCAGAGACCGGC TGAAGCTAGGTAAGCCTCTTGGCCGTGGTGCCTTTGGCCAAGTGATTGAA GCAGATGCCTTTGGAATTGACAAGACAGCAACTTGCAGGACAGTAGCAGT CAAAATGTTGAAAGAAGGAGCAACACACAGTGAGCATCGAGCTCTCATGT CTGAACTCAAGATCCTCATTCATATTGGTCACCATCTCAATGTGGTCAAC CTTCTAGGTGCCTGTACCAAGCCAGGAGGGCCACTCATGGTGATTGTGGA ATTCTGCAAATTTGGAAACCTGTCCACTTACCTGAGGAGCAAGAGAAATG AATTTGTCCCCTACAAGACCAAAGGGGCACGATTCCGTCAAGGGAAAGAC TACGTTGGAGCAATCCCTGTGGATCTGAAACGGCGCTTGGACAGCATCAC CAGTAGCCAGAGCTCAGCCAGCTCTGGATTTGTGGAGGAGAAGTCCCTCA GTGATGTAGAAGAAGAGGAAGCTCCTGAAGATCTGTATAAGGACTTCCTG ACCTTGGAGCATCTCATCTGTTACAGCTTCCAAGTGGCTAAGGGCATGGA GTTCTTGGCATCGCGAAAGTGTATCCACAGGGACCTGGCGGCACGAAATA TCCTCTTATCGGAGAAGAACGTGGTTAAAATCTGTGACTTTGGCTTGGCC CGGGATATTTATAAAGATCCAGATTATGTCAGAAAAGGAGATGCTCGCCT CCCTTTGAAATGGATGGCCCCAGAAACAATTTTTGACAGAGTGTACACAA TCCAGAGTGACGTCTGGTCTTTTGGTGTTTTGCTGTGGGAAATATTTTCC TTAGGTGCTTCTCCATATCCTGGGGTAAAGATTGATGAAGAATTTTGTAG GCGATTGAAAGAAGGAACTAGAATGAGGGCCCCTGATTATACTACACCAG AAATGTACCAGACCATGCTGGACTGCTGGCACGGGGAGCCCAGTCAGAGA CCCACGTTTTCAGAGTTGGTGGAACATTTGGGAAATCTCTTGCAAGCTAA TGCTCAGCAGGATGGCAAAGACTACATTGTTCTTCCGATATCAGAGACTT TGAGCATGGAAGAGGATTCTGGACTCTCTCTGCCTACCTCACCTGTTTCC TGTATGGAGGAGGAGGAAGTATGTGACCCCAAATTCCATTATGACAACAC AGCAGGAATCAGTCAGTATCTGCAGAACAGTAAGCGAAAGAGCCGGCCTG TGAGTGTAAAAACATTTGAAGATATCCCGTTAGAAGAACCAGAAGTAAAA GTAATCCCAGATGACAACCAGACGGACAGTGGTATGGTTCTTGCCTCAGA AGAGCTGAAAACTTTGGAAGACAGAACCAAATTATCTCCATCTTTTGGTG GAATGGTGCCCAGCAAAAGCAGGGAGTCTGTGGCATCTGAAGGCTCAAAC CAGACAAGCGGCTACCAGTCCGGATATCACTCCGATGACACAGACACCAC CGTGTACTCCAGTGAGGAAGCAGAACTTTTAAAGCTGATAGAGATTGGAG TGCAAACCGGTAGCACAGCCCAGATTCTCCAGCCTGACTCGGGGACCACA CTGAGCTCTCCTCCTGTTTAA VEGFR2 Protein Sequence (SEQ ID NO: 4) MQSKVLLAVALWLCVETRAASVGLPSYSLDLPRLSIQKDILTIKANTTLQ ITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGA YKCFYRETDLASVIYVYVQDYRSPFIASYSDQHGVVYITENKNKTVVIPC LGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFC EAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTART ELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRS DQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRI PAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVIL TNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAI PPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVN KNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRG PEITLQPDMQPTEQESYSLWCTADRSTFENLTWYKLGPQPLPIHVGELPT PVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTK KRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMW FKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEA FFIIEGAQEKTNLEIIILVGTAVIAMFFWLLLVIILRTVKRANGGELKTG YLSIVMDPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIE ADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVN LLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYKTKGARFRQGKD YVGAIPVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEAPEDLYKDFL TLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLA RDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFS LGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQR PTFSELVEHLGNLLQANAQQDGKDYIVLPISETLSMEEDSGLSLPTSPVS CMEEEEVCDPKFHYDNTAGISQYLQNSKRKSRPVSVKTFEDIPLEEPEVK VIPDDNQTDSGMVLASEELKTLEDRTKLSPSFGGMVPSKSRESVASEGSN QTSGYQSGYHSDDTDTTVYSSEEAELLKLIEIGVQTGSTAQILQPDSGTT LSSPPV The term “VEGF” may also be used to refer to truncated forms or fragments of the polypeptide comprising amino acids 8 to 109 or 1 to 109 of the 165-amino acid human vascular endothelial cell growth factor. The amino acid positions for a “truncated” native VEGF are numbered as indicated in the native VEGF sequence. For example, amino acid position 17 (methionine) in truncated native VEGF is also position 17 (methionine) in native VEGF. The truncated native VEGF has binding affinity for the KDR and Flt-1 receptors comparable to native sequence VEGF. A “VEGF antagonist” refers to a molecule (peptidyl or non-peptidyl) capable of neutralizing, blocking, inhibiting, abrogating, reducing or interfering with activities of a native sequence VEGF, including its binding to one or more VEGF receptors. VEGF antagonists include anti-VEGF antibodies and antigen-binding fragments thereof, receptor molecules and derivatives that bind specifically to VEGF, thereby sequestering its binding to one or more receptors (e.g., soluble VEGF receptor proteins or VEGF binding fragments thereof, or chimeric VEGF receptor proteins), anti-VEGF receptor antibodies and VEGF receptor antagonists, such as small molecule inhibitors of the VEGFR tyrosine kinases, and fusion proteins. VEGF antagonists according to embodiments may include antagonists of VEGF, antisense molecules directed to VEGF, RNA aptamers, and ribozymes against VEGF or VEGF receptors. VEGF antagonists useful in embodiments may further include peptidyl or non-peptidyl compounds that specifically bind VEGF, such as anti-VEGF antibodies and antigen-binding fragments thereof, polypeptides, antibody variants or fragments thereof that specifically bind to VEGF, antisense nucleic oligomers complementary to at least a fragment of a nucleic acid molecule encoding a VEGF polypeptide, small RNAs complementary to at least a fragment of a nucleic acid molecule encoding a VEGF polypeptide, ribozymes that target VEGF, peptibodies to VEGF, and VEGF aptamers. In embodiments, the VEGF antagonist reduces or inhibits, by at least 10%, or more, the expression level or biological activity of VEGF. The term “anti-VEGF antibody” or “an antibody that binds to VEGF” refers to an antibody that is capable of binding to VEGF with sufficient affinity and, specifically, that the antibody is useful as a diagnostic and/or therapeutic agent in targeting VEGF. In embodiments, the anti-VEGF antibody may be used as a therapeutic agent in targeting and interfering with diseases or conditions in which the VEGF activity is involved. The antibody selected will normally have a sufficiently strong binding affinity for VEGF, for example, the antibody may bind to human VEGF with a Kd value of between 100 nM-1 pM. Antibody affinities may be determined by a surface plasmon resonance based assay (such as the BIACORE assay described in PCT Application Publication No. WO 2005/012359), enzyme-linked immunoabsorbent assay (ELISA), and/or competition assays (e.g., RIAs). In embodiments, an anti-VEGF antibody may be substituted with a VEGF specific antagonist, e.g., a VEGF receptor molecule or chimeric VEGF receptor molecule as described herein. In certain embodiments, the anti-VEGF antibody is BEVACIZUMAB. The anti-VEGF antibody, or antigen-binding fragment thereof, can be a monoclonal antibody, a chimeric antibody, a fully human antibody, or a humanized antibody. The term “angiogenesis” or “neovascularization” refers to the process by which new blood vessels develop from pre-existing vessels. (Varner et al., Angiogen. 3(1):53-60 (1999); Mousa et al., Angiogenesis Stim. and Inhib., 35-42, 44 (2000)). Endothelial cells from pre-existing blood vessels or from circulating endothelial stem cells become activated to migrate, proliferate, and differentiate into structures with lumens, forming new blood vessels, in response to growth factor or hormonal cues, or hypoxic or ischemic conditions. (Takahashi et al., Nat. Med. 5:434-438 (1995)). During ischemia, such as occurs in cancer, the need to increase oxygenation and delivery of nutrients apparently induces the secretion of angiogenic factors by the affected tissue; and these factors stimulate new blood vessel formation. Several additional terms related to angiogenesis are defined below. As used herein, the term “inhibiting angiogenesis,” means reducing a level of angiogenesis in a tissue where angiogenesis is occurring, i.e., where new blood vessels are developing from pre-existing blood vessels. In embodiments, inhibiting angiogenesis refers to reducing the level of angiogenesis in a tumor (or cancer) to a level that is at least 10% lower than a level of angiogenesis in a corresponding control tissue, and preferably at least 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% lower than the level of angiogenesis in the corresponding control tissue. A reduced level of angiogenesis need not, although it may, mean an absolute absence of angiogenesis. The level of angiogenesis may be determined using methods well known in the art, including, e.g., counting the number of blood vessels and/or the number of blood vessel branch points, as discussed herein and in the examples. An alternative in vitro assay contemplated in some embodiments includes a tubular cord formation assay that shows growth of new blood vessels at the cellular level (D. S. Grant et al., Cell, 58:933-943 (1989)). Art-accepted in vivo assays that involve the use of various test animals, such as chickens, rats, mice, rabbits and the like may also be used. These in vivo assays include the chicken chorioallantoic membrane (CAM) assay, which is suitable for showing anti-angiogenic activity in both normal and neoplastic tissues (D. H. Ausprunk, Amer. J. Path. 79, No. 3:597-610 (1975); and L. Ossonowski and E. Reich, Cancer Res., 30:2300-2309 (1980)). Other conventional in vivo assays include the mouse metastasis assay, which demonstrates the ability of a compound to reduce the rate of growth of transplanted tumors in certain mice, or to inhibit the formation of tumors or preneoplastic cells in mice that are predisposed to cancer or that express chemically-induced cancer (M. J. Humphries et al., Science, 233:467-470 (1986); and M. J. Humphries et al., J. Clin. Invest. 81:782-790 (1988)). In some embodiments, angiogenesis can be measured according to attributes such as pericyte maturation and vascular remodeling, as described further herein. As used herein, the term “hypoxia associated angiogenesis” or “hypoxia-induced angiogenesis” refers generally to the process of pathological angiogenesis in non-neoplastic disease states and is typically, although not necessarily, accompanied by a transition to a neoplastic state. Hypoxia-induced transcription factors (HIFs) induce the expression of angiogenic factors, including HIF-1alpha, VEGF, nitric oxide synthase, PDFG, Ang2, and others. As a result, hypoxia associated angiogenesis encompasses a well-known set of pathological conditions characterized by such a process. See, e.g., Pugh et al., Nat. Med. 9, 677-684 (2003); Fraisl et al., Dev. Cell. 16, 167-179 (2009); Ferrara et al., Nature 438, 967-974 (2005); Ferrara, N., Cytokine Growth Factor Rev. 21, 21-26 (2010). In some embodiments, the set of hypoxia associated angiogenesis pathologies includes, but is not limited to, cancers. Unless otherwise specified in the disclosure, the terms “antibody” and “antibodies” broadly encompass naturally-occurring forms of antibodies (e.g., IgG, IgA, IgM, IgE), as well as recombinant antibodies (e.g., single-chain, humanized, and multi-specific antibodies) and fragments and derivatives of all of the foregoing, wherein such fragments and derivatives have at least an antigenic binding site. Antibody derivatives may comprise a protein or chemical moiety conjugated to an antibody. Generally, an “antibody” refers to a glycoprotein comprising at least two heavy (H) chains and two light (L) chains inter-connected by disulfide bonds, or an antigen binding portion thereof. Each heavy chain is comprised of a heavy chain variable region (abbreviated herein as VH) and a heavy chain constant region. The heavy chain constant region is comprised of three domains, CH1, CH2 and CH3. Each light chain is comprised of a light chain variable region (abbreviated herein as VL) and a light chain constant region. The light chain constant region is comprised of one domain, CL. The VH and VL regions can be further subdivided into regions of hypervariability, termed complementarity determining regions (CDR), interspersed with regions that are more conserved, termed framework regions (FR). Each VH and VL is composed of three CDRs and four FRs, arranged from amino-terminus to carboxy-terminus in the following order: FR1, CDR1, FR2, CDR2, FR3, CDR3, FR4. The variable regions of the heavy and light chains contain a binding domain that interacts with an antigen. The term “CDR,” and its plural “CDRs,” refers to a complementarity determining region (CDR) of which three make up the binding character of a light chain variable region (CDRL1, CDRL2 and CDRL3) and three make up the binding character of a heavy chain variable region (CDRH1, CDRH2 and CDRH3). CDRs contribute to the functional activity of an antibody molecule and are separated by amino acid sequences that comprise scaffolding or framework regions. An antibody or antigen-binding portion thereof may be part of a larger immunoadhesion polypeptide, formed by covalent or noncovalent association of the antibody or antibody portion with one or more other proteins or peptides. Antibody portions, such as Fab and F(ab′)2 fragments, can be prepared from whole antibodies using conventional techniques, such as papain or pepsin digestion, respectively, of whole antibodies. Moreover, antibodies, antibody portions and immunoadhesion polypeptides can be obtained using standard recombinant DNA techniques, as described herein. Antibodies may be polyclonal or monoclonal; xenogeneic, allogeneic, syngeneic, or modified forms thereof (e.g., humanized, chimeric, etc.). Antibodies may also be fully human. As used herein, the terms “monoclonal antibodies” and “monoclonal antibody composition” refer to a population of antibody polypeptides that contain only one species of an antigen binding site capable of immunoreacting with a particular epitope of an antigen, whereas the term “polyclonal antibodies” and “polyclonal antibody composition” refer to a population of antibody polypeptides that contain multiple species of antigen binding sites capable of interacting with a particular antigen. In embodiments, antibodies may bind specifically or substantially specifically to Gal1 or VEGF2 polypeptides or fragments thereof. Accordingly, the term “human monoclonal antibody” refers to an antibody that displays a single binding specificity and that has variable and constant regions derived from human germline or non-germline immunoglobulin sequences. In some embodiments, human monoclonal antibodies may be produced by a hybridoma that includes a B cell obtained from a transgenic non-human animal, e.g., a transgenic mouse, having a genome comprising a human heavy chain transgene and a light chain transgene fused to an immortalized cell. In embodiments, antibodies may bind specifically or substantially specifically to Gal1 or VEGF2 polypeptides or fragments thereof. The term “humanized antibody,” as used herein, includes antibodies made by a non-human cell having variable and constant regions that have been altered to more closely resemble antibodies that would be made by a human cell, e.g., by altering a non-human antibody amino acid sequence to incorporate amino acids found in human germline immunoglobulin sequences. In embodiments, humanized antibodies may include amino acid residues not encoded by human germline immunoglobulin sequences (e.g., mutations introduced by random or site-specific mutagenesis in vitro or by somatic mutation in vivo), for example in the CDRs. As used herein, the term “humanized antibody” also includes antibodies in which CDR sequences derived from the germline of another mammalian species, such as a mouse, have been grafted onto human framework sequences. As used herein, the term “recombinant human antibody” includes all human antibodies that are prepared, expressed, created or isolated by recombinant means, such as, for example: (a) antibodies isolated from an animal (e.g., a mouse) that is transgenic or transchromosomal for human immunoglobulin genes, or a hybridoma prepared as described further below; (b) antibodies isolated from a host cell transformed to express the antibody, e.g., from a transfectoma; (c) antibodies isolated from a recombinant, combinatorial human antibody library; and (d) antibodies prepared, expressed, created or isolated by any other means that involve splicing of human immunoglobulin gene sequences to other DNA sequences. Such recombinant human antibodies have variable and constant regions derived from human germline and/or non-germline immunoglobulin sequences. In certain embodiments, however, such recombinant human antibodies can be subjected to in vitro mutagenesis (or, when an animal transgenic for human Ig sequences is used, in vivo somatic mutagenesis) and thus the amino acid sequences of the VH and VL regions of the recombinant antibodies are sequences that, while derived from and related to human germline VH and VL sequences, may not naturally exist within the human antibody germline repertoire in vivo. As used herein, the term “heterologous antibody” is defined in relation to a transgenic non-human organism producing such an antibody. This term refers to an antibody having an amino acid sequence or an encoding nucleic acid sequence corresponding to that found in an organism not consisting of the transgenic non-human animal, and generally from a species other than the transgenic non-human animal. As used herein, an “isolated antibody” is intended to refer to an antibody that is substantially free of other antibodies having different antigenic specificities (e.g., an isolated antibody that specifically binds to human Gal1 and is substantially free of antibodies that do not bind to Gal1). An isolated antibody that specifically binds to an epitope of human Gal1 may, however, have cross-reactivity to other Gal1 proteins, respectively, from different species. However, in some embodiments, the antibody maintains higher affinity and selectivity for human Gal1. In addition, an isolated antibody is typically substantially free of other cellular material and/or chemicals. In certain embodiments, a combination of “isolated” monoclonal antibodies having different specificities to human Gal1 may be included in a defined composition. As used herein, the term “hypervariable region,” “HVR,” or “HV,” refers to a region of an antibody-variable domain that is hypervariable in sequence and/or forms structurally defined loops. Generally, antibodies comprise six HVRs; three in the VH (H1, H2, H3), and three in the VL (L1, L2, L3). In native antibodies, H3 and L3 display the most diversity of the six HVRs, and H3 in particular is believed to play a unique role in conferring fine specificity to antibodies. See, e.g., Xu et al. Immunity 13, 37-45
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