Type XV collagen in human colonic adenocarcinomas has a different distribution than other basement membrane zone proteins

Amenta, Peter S.; Briggs, Kari; Xu, Karen; Gamboa, Elmer; Jukkola, Alina F.; Li, Deqin; Myers, Jeanne C.

doi:10.1016/s0046-8177(00)80251-8

Cited by 40 publications

(31 citation statements)

References 38 publications

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“…Ultrastructural localization of type XV collagen in placenta was consistent with the kidney results, and the same distribution pattern was observed using type XV antibodies raised against the carboxyor amino-terminal domains (Myers et al 1996(Myers et al ,1997Amenta et al 2000;Li et al 2000). Type XV was most prevalent within the stroma immediately adjacent to either the trophoblastic ( Figure 4A) or endothelial BM (data not shown).…”

Section: Immunogold Localization Of Type XV Collagen In Human Tissuessupporting

confidence: 83%

“…The localization of type XV collagen clarifies former light microscopy studies, which showed its distribution in colon and breast carcinomas to be significantly different from integral BM components (Amenta et al 2000(Amenta et al ,2003. Type XV was lost from the BM zone early in the invasive process, before fragmentation of the BM as evidenced by linear immunoreactivity for type IV collagen and laminin.…”

Section: Type XV May Help To Protect Collagen Fibers From Proteolysissupporting

confidence: 81%

“…Development and characterization of the polyclonal type XV carboxy and amino antibodies have been described previously (Myers et al 1996(Myers et al ,1997Li et al 2000;Amenta et al 2000Amenta et al ,2003.…”

Section: Type XV Collagen Antibodiesmentioning

confidence: 99%

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Proteoglycan-Collagen XV in Human Tissues Is Seen Linking Banded Collagen Fibers Subjacent to the Basement Membrane

Amenta

Scivoletti

Newman

et al. 2005

J Histochem Cytochem.

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S U M M A R YType XV is a large collagen-proteoglycan found in all human tissues examined. By light microscopy it was localized to most epithelial and all nerve, muscle, fat and endothelial basement membrane zones except for the glomerular capillaries or hepatic/ splenic sinusoids. This widespread distribution suggested that type XV may be a discrete structural component that acts to adhere basement membrane to the underlying connective tissue. To address these issues, immunogold ultrastructural analysis of type XV collagen in human kidney, placenta, and colon was conducted. Surprisingly, type XV was found almost exclusively associated with the fibrillar collagen network in very close proximity to the basement membrane. Type XV exhibited a focal appearance directly on the surface of, or extending from, the fibers in a linear or clustered array. The most common single arrangement was a bridge of type XV gold particles linking thick-banded fibers. The function of type XV in this restricted microenvironment is expected to have an intrinsic dependence upon its modification with glycosaminoglycan chains. Present biochemical characterization showed that the type XV core protein in vivo carries chains of chondroitin/dermatan sulfate alone, or chondroitin/dermatan sulfate together with heparan sulfate in a differential ratio. Thus, type XV collagen may serve as a structural organizer to maintain a porous meshwork subjacent to the basement membrane, and in this domain may play a key role in signal transduction pathways. (J Histochem Cytochem 53: [165][166][167][168][169][170][171][172][173][174][175][176] 2005)

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Section: Immunogold Localization Of Type XV Collagen In Human Tissuessupporting

confidence: 83%

Section: Type XV May Help To Protect Collagen Fibers From Proteolysissupporting

confidence: 81%

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Proteoglycan-Collagen XV in Human Tissues Is Seen Linking Banded Collagen Fibers Subjacent to the Basement Membrane

Amenta

Scivoletti

Newman

et al. 2005

J Histochem Cytochem.

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“…The top-signal SNP, rs1413299, is in intron 6 of COL15A1 that encodes the a-chain of type XV collagen at 9q22.33, a member of the FACIT (fibril-associated collagens with interrupted helices) collagen family. Loss of the COL15A1 protein from the basement membranes/basement membrane zone was reported to promote tumour cell infiltration in human ductal breast carcinoma cells and colon carcinomas 19,20 . In addition, COL15A was found to suppress tumorigenesis in a dosedependent manner in human cervical carcinoma cell line 21 .…”

Section: Discussionmentioning

confidence: 99%

Genome-wide association study identifies new susceptibility loci for epithelial ovarian cancer in Han Chinese women

Chen

et al. 2014

Nat Commun

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Ovarian cancer is the leading cause of death from gynaecological malignancies worldwide. Here we perform a three-stage genome-wide association study (GWAS) in Han Chinese women to identify risk genetic variants for epithelial ovarian cancer (EOC). We scan 900,015 single-nucleotide polymorphisms (SNPs) in 1,057 EOC cases and 1,191 controls in stage I, and replicate 41 SNPs (P meta o10 À 4 ) in 960 EOC cases and 1,799 controls (stage II), and an additional 492 EOC cases and 1,004 controls (stage III). Finally, we identify two EOC susceptibility loci at 9q22.33 (rs1413299 in COL15A1, P meta ¼ 1.88 Â 10 À 8 ) and 10p11.21 (rs1192691 near ANKRD30A, P meta ¼ 2.62 Â 10 À 8 ), and two consistently replicated loci at 12q14.2 (rs11175194 in SRGAP1, P meta ¼ 1.14 Â 10 À 7 ) and 9q34.2 (rs633862 near ABO and SURF6, P meta ¼ 8.57 Â 10 À 7 ) (Po0.05 in all three stages). These results may advance our understanding of genetic susceptibility to EOC.

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“…It has been proposed that collagen XV may be involved in the invasiveness of tumors because it is lost in the malignant epithelial basement membranes of colonic adenocarcinomas and ductal carcinomas (3,4) and because melanocytic nevi and malignant melanomas in situ were positive for collagen XV, whereas melanomas with dermal invasion were negative (5). Recent studies with collagen XV and XVIII double null mice have indicated that collagen XV may also have a regulatory role in inhibiting the migration of astrocytes (6).…”

mentioning

confidence: 99%

Recombinant Human Collagen XV Regulates Cell Adhesion and Migration

Hurskainen

Ruggiero

Hägg

et al. 2010

Journal of Biological Chemistry

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The C-terminal end of collagen XV, restin, has been the focus of several studies, but the functions of full-length collagen XV have remained unknown. We describe here studies on the production, purification, and function of collagen XV and the production of a monoclonal N-terminal antibody to it. Full-length human collagen XV was produced in insect cells using baculoviruses and purified from the cell culture medium. The yield was 15 mg/liter of cell culture medium. The collagen XV was shown to be trimeric, with disulfide bonds in the collagenous region. Rotary shadowing electron microscopy revealed rod-like molecules with a mean length of 241.8 nm and with a globular domain at one end. The globular domain was verified to be the N-terminal end by N-terminal antibody binding. The molecules show flexibility in their conformation, presumably due to the many interruptions in their collagenous domains. The ability of collagen XV to serve as a substrate for cells was tested in cell adhesion assays, and it was shown that cells did not bind to collagen XVcoated surfaces. When added to the culture medium of fibroblasts and fibrosarcoma cells, however, collagen XV rapidly bound to their fibronectin network. Solid phase assays showed that collagen XV binds to fibronectin, laminin, and vitronectin and that it binds to the collagen/gelatin-binding domain of fibronectin. No binding was detected to fibrillar collagens, fibril-associated collagens, or decorin. Interestingly, collagen XV was found to inhibit the adhesion and migration of fibrosarcoma cells when present in fibronectin-containing matrices.Lack of collagen XV in mice leads to the development of skeletal myopathy, collapsed capillaries, and degenerating endothelial cells in the heart and skeletal muscles, suggesting that collagen XV may be important for linking basement membranes to their surrounding tissues (1). Indeed, EM 2 studies have indicated that collagen XV links banded collagen fibers to basement membranes (2).It has been proposed that collagen XV may be involved in the invasiveness of tumors because it is lost in the malignant epithelial basement membranes of colonic adenocarcinomas and ductal carcinomas (3, 4) and because melanocytic nevi and malignant melanomas in situ were positive for collagen XV, whereas melanomas with dermal invasion were negative (5). Recent studies with collagen XV and XVIII double null mice have indicated that collagen XV may also have a regulatory role in inhibiting the migration of astrocytes (6).Collagen XV is a non-fibrillar collagen widely distributed in various tissues, where it has been shown to localize to the basement membrane zones (7-9). Human collagen XV is a homotrimer with ␣ chains composed of 1363 amino acid residues containing a highly interrupted collagenous domain of 577 amino acids flanked by large non-collagenous N-and C-terminal domains of 530 and 256 amino acids, respectively (10, 11). Collagen XV shares structural homology with collagen XVIII, and they together form a subgroup of collagens with their highest ...

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Type XV collagen in human colonic adenocarcinomas has a different distribution than other basement membrane zone proteins

Cited by 40 publications

References 38 publications

Proteoglycan-Collagen XV in Human Tissues Is Seen Linking Banded Collagen Fibers Subjacent to the Basement Membrane

Proteoglycan-Collagen XV in Human Tissues Is Seen Linking Banded Collagen Fibers Subjacent to the Basement Membrane

Genome-wide association study identifies new susceptibility loci for epithelial ovarian cancer in Han Chinese women

Recombinant Human Collagen XV Regulates Cell Adhesion and Migration

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