Binding of laminin to type IV collagen: a morphological study.

Charonis, Aristidis S.; Tsilibary, Effie C.; Yurchenco, Peter D.; Furthmayr, Heinz

doi:10.1083/jcb.100.6.1848

Cited by 177 publications

(71 citation statements)

References 22 publications

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“…Self-assembly of type IV collagen can also proceed laterally via its triple helical regions or via binding of the non-collagenous domain to the triple helical region of another molecule to form multimers (27,29). Studies examining the interaction of laminin and heparin with type IV collagen demonstrated that both molecules show significant binding to the triple helical region of type IV collagen (28,30). Since SAP binding to type IV collagen is most likely via type IV collagen's triple helical region, it may modify the assembly of type IV collagen or its interaction with proteoglycans and laminin and alter the structure of the basement membrane and its function.…”

Section: Fig 7 Effect Of Camentioning

confidence: 99%

Characterization of the Binding of Serum Amyloid P to Type IV Collagen

Zahedi¹

1996

Journal of Biological Chemistry

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Serum amyloid P (SAP)1 is a 10-subunit (two flat pentameric discs stacked face to face) M r Ϸ 230,000 glycoprotein coded by a single gene on human and mouse chromosome 1 (1, 2). It is a member of the evolutionarily conserved pentraxin family (1). These are proteins that are made up of five identical noncovalently bound subunits arranged in a flat pentameric disc (1, 3). In vitro SAP binds to proteoglycans and fibronectin in a specific Ca 2ϩ -dependent manner (4 -6). Furthermore, SAP binds to the collagen-like region of complement component C1q (7). SAP is a normal component of a group of basement membranes including glomerular and alveolar basement membranes (8, 9). It comprises approximately 10% of the protein released from glomerular basement membrane after collagenase treatment (8). Association of SAP with glomerular basement membranes is completely disrupted or disturbed in a number of nephritides such as Alport's syndrome (10), membranous glomerulonephritis, and membranoproliferative glomerulonephritis (11).Basement membranes are multicomponent structures that perform a variety of functions. They are involved in maintenance of the differentiated state and basal and apical polarity of the cells as well as maintenance of the organ structure and filtration functions (12, 13). A number of factors affect the structure and function of basement membranes (e.g. the relative concentration of each component and the affinity of the interaction between components as well as their structure) (14 -16). It is therefore possible that SAP, via its interaction with various components of the extracellular matrix, modifies the structure and function of the basement membranes with which it is associated. In the present study, the binding of SAP to type IV collagen was examined. The data indicate that SAP binding to type IV collagen is Ca 2ϩ -dependent, specific and saturable with a K d Ϸ 1.2 ϫ 10 Ϫ7 M for immobilized and a K d Ϸ 4 ϫ 10 Ϫ8 M (based on the IC 50 value of the soluble phase binding assay) for soluble type IV collagen. Furthermore, SAP probably binds via its C1q binding region to the triple helical region of type IV collagen. The interaction of SAP with type IV collagen and other components of the basement membrane may affect the structure of the basement membranes, thereby affecting their function. EXPERIMENTAL PROCEDURESMaterials-Human SAP and CRP were purchased from Calbiochem. Each protein gave a single band of M r Ϸ 23,000 and 25,000 when size fractionated on SDS-polyacrylamide gel (12% polyacrylamide) under reducing conditions. Mouse SAP was purified from acute phase mouse serum (provided by R. F. Mortensen, Ohio State University) by Ca 2ϩ -dependent affinity chromatography on a column of phosphatidylethanolamine conjugated to agarose beads (Sigma) as described previously (17) followed by anion exchange chromatography on a Mono Q column (Pharmacia Biotech Inc.). The purified protein gave a single band of M r Ϸ 23,000 upon size fractionation on SDS-polyacrylamide gel electrophoresis (12% polyacrylamide) under r...

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Section: Fig 7 Effect Of Camentioning

confidence: 99%

Characterization of the Binding of Serum Amyloid P to Type IV Collagen

Zahedi¹

1996

Journal of Biological Chemistry

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“…There is evidence that the latter are distributed in most basement membranes (4,5). Type IV collagen not only forms the main structural framework of all basement membranes, but also serves as scaffolding for the binding of other basement membrane components (7,8). One important function of type IV collagen is its ability to promote the adhesion and motility of various normal and transformed cell types (9).…”

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confidence: 99%

A Cell Binding Domain from the α3 Chain of Type IV Collagen Inhibits Proliferation of Melanoma Cells

Han¹,

Ohno²,

Brassart‐Pasco³

et al. 1997

Journal of Biological Chemistry

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Our previous studies have shown that a peptide corresponding to the residue sequence 185-203 of the NC1 domain of the ␣3 chain of basement membrane collagen (type IV) inhibits the activation of polymorphonuclear leukocytes. Peptides from the same region of the ␣1, ␣2, ␣4, and ␣5(IV) chains did not exhibit this property. Because of the intimate relationship between metastasizing neoplastic cells and vascular as well as epithelial basement membranes, we measured the cell adhesionpromoting activity of peptides from the NC1 domain of type IV collagen and their effect on proliferation of human melanoma cells. We found that peptide ␣3(IV)185-203 (CNYYSNSYSFWLASLNPER) not only promotes adhesion of human melanoma cells but also inhibits their proliferation. Adhesion increased by 50 -60% over control. Melanoma cell proliferation was inhibited by 40% when cells were grown in a medium containing 5 g/ml peptide for 5 days. Studies showed that replacement of serine in position 189 or 191 by alanine resulted in significantly reduced adhesion. Similarly, serine replacement resulted in reduced ability to inhibit proliferation. Our data suggest that a region of the NC1 domain of the ␣3(IV) chain, contained within the sequence 185-203, not only specifically promotes adhesion but also inhibits proliferation of melanoma cells. These properties appear to be dependent on the presence of the triplet sequence -SNS-(residues 189 -191), which is unique to the ␣3 chain and may represent an important functional epitope.

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“…This collagen is unique to basement membrane and forms large open or polygonal networks [31,32]. This network forms a scaffolding to which other proteins bind at specific sites [33][34][35]. Entactin is involved in the binding of laminin to collagen type IV [36].…”

Section: Discussionmentioning

confidence: 99%

Reconstituted basement membrane (matrigel) enhances the growth of human glioma cell lines in nude mice

1996

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Transplantation of human cancers into immunologically deficient mice is widely used to study potential therapeutic interventions in vivo. For brain tumor research, however, several factors limit more widespread application of this animal model. First, only a minority of human glioma-derived cell lines are tumorigenic in nude mice. In addition, even for tumorigenic cell lines, tumor take is variable and growth is often slow for tumors derived from cell inoculums. Reconstituted components of tumor basement membrane (matrigel) have been found to improve the growth in nude mice of several types of human tumors originating outside the central nervous system when premixed with the tumor cells before subcutaneous inoculation. We investigated the ability of matrigel to enhance the growth in nude mice of tumors derived from the human glioma cell lines U-251 MG, U-373 MG, SNB-78 and SNB-101. Athymic nude mice (NIH Swiss background, nu/nu genotype) were inoculated subcutaneously with 1.0 x 10(6) tumor cells alone or after premixing with an equal volume of liquid matrigel. U-251 and U-373 cells were tumorigenic, with palpable tumors present by about 2 to 3 weeks. Co-injection of these cell lines with matrigel resulted in higher tumor-take rates, from 6/10 to 8/8 animals for U-251 at 60 days, and from 9/12 to 11/11 animals for U-373 at 60 days. Matrigel also enhanced tumor growth, with tumors at 45 days significantly larger than those formed in the absence of matrigel, for both cell lines (p < 0.01). SNB-78 and SNB-101 cells did not give rise to progressively enlarging solid tumors with or without matrigel. Matrigel enhances the growth of tumorigenic human gliomas in athymic nude mice. This technique provides a model with more consistent tumor take and more rapid growth kinetics for human glioma cell lines that are tumorigenic in nude mice.

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Binding of laminin to type IV collagen: a morphological study.

Cited by 177 publications

References 22 publications

Characterization of the Binding of Serum Amyloid P to Type IV Collagen

Characterization of the Binding of Serum Amyloid P to Type IV Collagen

A Cell Binding Domain from the α3 Chain of Type IV Collagen Inhibits Proliferation of Melanoma Cells

Reconstituted basement membrane (matrigel) enhances the growth of human glioma cell lines in nude mice

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