Cell type specific recognition of the reconstituted aggregates from isolated type I collagen, type IV collagen, and type V collagen

In the past it has been proven difficult to separate and characterize collagen from muscle because of its relative paucity in this tissue. The present report presents a comprehensive methodology, combining methods previously described by McCollester [(1962) Biochim. Biophys. Acta 57, 427-437] and Laurent, Cockerill, McAnulty & Hastings [(1981) Anal. Biochem. 113, 301-312], in which the three major tracts of muscle connective tissue, the epimysium, perimysium and endomysium, may be prepared and separated from the bulk of muscle protein. Connective tissue thus prepared may be washed with salt and treated with pepsin to liberate soluble native collagen, or can be washed with sodium dodecyl sulphate to produce a very clean insoluble collagenous product. This latter type of preparation may be used for quantification of the ratio of the major genetic forms of collagen or for measurement of reducible cross-link content to give reproducible results. It was shown that both the epimysium and perimysium contain type I collagen as the major component and type III collagen as a minor component; perimysium also contained traces of type V collagen. The endomysium, the sheaths of individual muscle fibres, was shown to contain both type I and type III collagen as major components. Type V collagen was also present in small amounts, and type IV collagen, the collagenous component of basement membranes, was purified from endomysial preparations. This is the first biochemical demonstration of the presence of type IV collagen in muscle endomysium. The preparation was shown to be very similar to other type IV collagens from other basement membranes on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and was indistinguishable from EHS sarcoma collagen and placenta type IV collagen in the electron microscope after rotary shadowing.

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Platelet Collagen Activation by Basement Membrane Collagens

10.1055/s-0039-1684661 ◽

1979 ◽

Author(s):

L. Balleisen ◽

J. Rauterberg

Keyword(s):

Basement Membrane ◽

Collagen Type ◽

Normal Subjects ◽

Collagen Type I ◽

Short Chain ◽

Collagen Type Iv ◽

Type I ◽

Type Iv ◽

Aggregation Activity ◽

Type V

The collagen component of the vessel intima consists of collagen type I, III and basement membrane collagens. For type III a particularly potent platelet aggregation activity was found earlier.Three different basement membrane collagens were isolated from call placenta. Occurence of type IV and V(A/B collagen) in the intimal and medial layer of vessel walls has been shown by chemical and immunhistological means(1). The third basement membrane collagen is probably isentical with the 55000 molecular weight component described by CHUNG et al. (2).Platelets from normal subjects were tested for aggregation and spreading on Zaponlack with type IV, V, the separated A and B chains of type V and the short chain collagen. Complete aggregation was obtained only with native type V collagen. Spreading of platelets was induced only by collagen type IV, the A chain of type V and the short chain collagen.The data indicate that all basement membrane collagens activate platelets but in different respects.1. Rauterberg J. et al.: Coll. Int. Cent. Nat. Rech. Sc. 287:220(1978)2. Chung E. et al.: Bioehem. Biophys. Res. Comm. 71: 1167(1976)

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Distribution of laminin, collagen type IV, collagen type I, and fibronectin in chicken cardiac jelly/basement membrane

The Anatomical Record ◽

10.1002/ar.1092240310 ◽

1989 ◽

Vol 224 (3) ◽

pp. 417-425 ◽

Cited By ~ 41

Author(s):

Charles D. Little ◽

Dominique M. Piquet ◽

Lynn A. Davis ◽

Luanne Walters ◽

Christopher J. Drake

Keyword(s):

Basement Membrane ◽

Type Iv Collagen ◽

Collagen Type ◽

Collagen Type I ◽

Collagen Type Iv ◽

Type I ◽

Type Iv

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Laminin potentiates differentiation of PCC4uva embryonal carcinoma into neurons

Journal of Cell Science ◽

10.1242/jcs.97.1.23 ◽

1990 ◽

Vol 97 (1) ◽

pp. 23-31

Author(s):

T.M. Sweeney ◽

R.C. Ogle ◽

C.D. Little

Keyword(s):

Retinoic Acid ◽

Neural Differentiation ◽

Type Iv Collagen ◽

Embryonal Carcinoma ◽

Type I Collagen ◽

Collagen Type ◽

Collagen Type I ◽

Response To Treatment ◽

Type I ◽

Type Iv

The embryonal carcinoma PCC4uva differentiates into neurons in response to treatment with retinoic acid and dbcAMP. We used this in vitro model system to study the effects of laminin on early neural differentiation. Laminin substrata markedly potentiate neural differentiation of retinoic acid and dbcAMP-treated cultures. Only laminin induced more rapid neural cell body clustering, neurite growth and neurite fasciculation as compared to type IV collagen, type I collagen, and fibronectin substrata. Exogenous laminin substrata promoted greater cell attachment, cellular spreading and growth to confluence than type IV collagen, type I collagen, fibronectin and glass substrata. Laminin-induced effects were inhibited by addition of laminin antibodies or the synthetic laminin-derived peptide Ile-Gly-Ser-Arg-NH2 (YIGSR-NH2). Treatment with YIGSR-NH2 also inhibited neural differentiation in the absence of exogenous laminin substrata, whereas synthetic peptides containing the RGD sequence and a control peptide YIGSK-NH2 showed no inhibitory effects. These results are consistent with the hypothesis that specific interactions between an early differentiating cell population(s) and extracellular laminin are required during neural differentiation.

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Alpha v beta 1 is a receptor for vitronectin and fibrinogen, and acts with alpha 5 beta 1 to mediate spreading on fibronectin

Journal of Cell Science ◽

10.1242/jcs.108.3.1227 ◽

1995 ◽

Vol 108 (3) ◽

pp. 1227-1238 ◽

Cited By ~ 1

Author(s):

J.F. Marshall ◽

D.C. Rutherford ◽

A.C. McCartney ◽

F. Mitjans ◽

S.L. Goodman ◽

...

Keyword(s):

Type I Collagen ◽

Collagen Type ◽

Collagen Type I ◽

Collagen Type Iv ◽

Type I ◽

Vitronectin Receptor ◽

Type Iv ◽

Beta 1 Integrin ◽

Alpha V Beta 3 ◽

Blocking Antibodies

We have shown previously that VUP was the only line out of ten human melanoma lines that failed to express the vitronectin receptor alpha v beta 3, but instead expressed alpha v beta 1. Levels of alpha v beta 1 expression were low on parental VUP cells so that iterative sorting by FACS, using an anti-alpha v antibody (13C2), was utilised to derive sublines with 8- to 10-fold higher amounts of cell surface alpha v beta 1. There was little difference between low (V-) and high (V+) alpha v beta 1-expressing sublines with regard to adherence to collagen type I, collagen type IV or laminin substrata. However, adherence to vitronectin and fibrinogen correlated closely with alpha v beta 1 expression (35-42% adhesion for V(+) lines versus 6–8% adhesion for V- lines on vitronectin, for example). Utilising a high alpha v beta 1-expressing subline (V + B2) we have shown that binding to vitronectin and fibrinogen was inhibited specifically by function-blocking antibodies to alpha v (17E6 and 14D9) and beta 1 (A11B2). V(+) sublines spread more compared with V(-) sublines on both vitronectin and fibronectin. However, neither alpha 5- nor alpha v-blocking antibodies had any effect on attachment or spreading of V + B2 on fibronectin whereas the combination of alpha 5 (PID6)- and alpha v(17E6)-blocking antibodies abrogated binding to fibronectin almost completely. This is the first report of an alpha v beta 1 integrin able to recognize vitronectin and fibrinogen, and also cooperate with alpha 5 beta 1 to mediate attachment to and spreading on fibronectin.

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Transforming Growth Factor-Beta Binds Reversibly in Vitro to Guglielmi Detachable Coils

Interventional Neuroradiology ◽

10.1177/159101999800400102 ◽

1998 ◽

Vol 4 (1) ◽

pp. 21-26 ◽

Cited By ~ 2

Author(s):

D.F. Kallmes ◽

G.R. Hankins ◽

M.K. Borland ◽

H.J. Cloft ◽

M.E. Jensen ◽

...

Keyword(s):

Growth Factor ◽

Type Iv Collagen ◽

Type I Collagen ◽

Transforming Growth Factor ◽

Absolute Amount ◽

Collagen Type Iv ◽

Type I ◽

Guglielmi Detachable Coils ◽

Type Iv ◽

Detachable Coils

We determined the propensity for and reversibility of transforming growth factor-ß (TGFß) binding to uncoated Guglielmi Detachable Coils (GDC) and to GDC coated with extracellular matrix (ECM) proteins. Three 1.0 centimetre samples each of uncoated GDC-18 and of GDC-18 coated with either poly-L-lysine, laminin, type I collagen, type IV collagen, fibronectin, or poly-L-lysine and laminin were prepared. These samples were immersed briefly in a solution containing I125-labelled TGFß at a concentration of 0.225 μg/ml with initial specific activity of 123.3 mCi/mg (DuPont-NEN, Billerica, MA), and were counted using a scintillation counter. Each sample was then placed in a vial containing saline, shaken for 60 seconds, and counted again. Selected samples were immersed for varying periods within the TGFß solution and counted before and after saline rinse. Samples were rinsed one week after initial rinsing and counted again. The amount of binding between coil types was compared using the Student t test. For all samples initial binding of TGFß was in the order of 60–120 pg/cm. For the pre-rinse data there were no statistically significant differences between the amount bound to any single coil coating type relative to other coatings. Compared to the initial accumulations, the amount remaining after rinsing ranged from 40% (poly-L-lysine) to 63% (poly-L-lysine with laminin), with a mean of 55% among the seven coil types. After rinsing there was more growth factor remaining on uncoated coils than on poly-L-lysine-coated coils (p=0.05), fibronectin-coated coils (p=0.01), and type IV collagen-coated coils (p=0.04). There was a trend toward greater residual growth factor on coils coated with poly-L-lysine and laminin compared to coils coated with poly-L-lysine alone (p=0.10). Delayed, second rinsing of the samples one week after initial testing demonstrated only minor incremental loss of TGFß from the coil surfaces. After five minutes of immersion, accumulation was approximately 200% greater than that noted with brief submersion, but immersions lasting over five minutes did not yield increasing levels of TGFß binding. TGFß binds to GDC coils. Binding is not improved with ECM protein-coated coils compared to uncoated coils. The absolute amount of TGFß bound to the coil will likely result in local concentrations of growth factor in the order of those required for biological activity in vivo.

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Cooperativity between Sertoli cells and testicular peritubular cells in the production and deposition of extracellular matrix components.

The Journal of Cell Biology ◽

10.1083/jcb.100.6.1941 ◽

1985 ◽

Vol 100 (6) ◽

pp. 1941-1947 ◽

Cited By ~ 218

Author(s):

M K Skinner ◽

P S Tung ◽

I B Fritz

Keyword(s):

Extracellular Matrix ◽

Sertoli Cells ◽

Type Iv Collagen ◽

Type I Collagen ◽

Collagen Type Iv ◽

Type I ◽

Type Iv ◽

Extracellular Matrix Components ◽

Extracellular Fibrils ◽

Peritubular Cells

We examined the synthesis and deposition of extracellular matrix (ECM) components in cultures of Sertoli cells and testicular peritubular cells maintained alone or in contact with each other. Levels of soluble ECM components produced by populations of isolated Sertoli cells and testicular peritubular cells were determined quantitatively by competitive enzyme-linked immunoabsorbent assays, using antibodies shown to react specifically with Type I collagen, Type IV collagen, laminin, or fibronectin. Peritubular cells in monoculture released into the medium fibronectin (432 to 560 ng/microgram cell DNA per 48 h), Type I collagen (223 to 276 ng/microgram cell DNA per 48 h), and Type IV collagen (350 to 436 ng/microgram cell DNA per 48 h) during the initial six days of culture in serum-free medium. In contrast, Sertoli cells in monoculture released into the medium Type IV collagen (322 to 419 ng/microgram cell DNA per 48 h) but did not form detectable amounts of Type I collagen or fibronectin during the initial six days of culture. Neither cell type produced detectable quantities of soluble laminin. Immunocytochemical localization investigations demonstrated that peritubular cells in monoculture were positive for fibronectin, Type I collagen, and Type IV collagen but negative for laminin. In all monocultures most of the ECM components were intracellular, with scant deposition as extracellular fibrils. Sertoli cells were positive immunocytochemically for Type IV collagen and laminin but negative for fibronectin and Type I collagen. Co-cultures of peritubular cells and Sertoli cells resulted in interactions that quantitatively altered levels of soluble ECM components present in the medium. This was correlated with an increased deposition of ECM components in extracellular fibrils. The data correlated with an increased deposition of ECM components in extracellular fibrils. The data presented here we interpret to indicate that the two cell types in co-culture act cooperatively in the formation and deposition of ECM components. Results are discussed with respect to the nature of interactions between mesenchymal peritubular cell precursors and adjacent epithelial Sertoli cell precursors in the formation of the basal lamina of the seminiferous tubule.

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