Formation of collagen fibrils by enzymic cleavage of precursors of type I collagen in vitro.

Miyahara, Michinori; Hayashi, Kazushi; Berger, Joel; Tanzawa, Kazuhiko; Njieha, F K; Trelstad, Robert L.; Prockop, Darwin J.

doi:10.1016/s0021-9258(17)42783-9

Cited by 90 publications

(13 citation statements)

References 38 publications

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“…In vitro fiber formation observed during pN-type I to type I collagen conversion demonstrated a dependence of the rate of fibril formation upon the rate of removal of the aminoterminal peptide, but the final fibril diameter was unaffected. In similar experiments using pC-type I collagen, the fibril formed concurrent with removal of the carboxyl-terminal peptide were of very large diameter (Miyahara et al, 1984). These observations suggest that the amino and carboxyl propeptides of both types I and III collagens may be directly involved in regulating fibril growth.…”

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confidence: 65%

“…A number of regulatory mechanisms have been suggested. These include direct participation by cells in fibrillogenesis (Birk and Trelstad, 1986) as well as the involvement of posttranslational proteolytic processing of type I and III procollagens (Miyahara et al, 1984;Fleischmajer et al, 1985) and possibly type V collagen (Fitch et al, 1984) in the control of this process. The latter postulates are supported by the observations that types I, III, and V collagens share common structural features (Miller, 1985), and that all can form fibrils in vitro with the same periodic D-banding seen in vivo (Adachi and Hayashi, 1985).…”

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confidence: 99%

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Type III collagen can be present on banded collagen fibrils regardless of fibril diameter.

Keene

Sakai

Bächinger

et al. 1987

The Journal of Cell Biology

250

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Abstract. Monoclonal antibodies that recognize an epitope within the triple helix of type HI collagen have been used to examine the distribution of that collagen type in human skin, cornea, amnion, aorta, and tendon. Ultrastructural examination of those tissues indicates antibody binding to collagen fibrils in skin, amnion, aorta, and tendon regardless of the diameter of the fibril. The antibody distribution is unchanged with donor age, site of biopsy, or region of tissue examined. In contrast, antibody applied to adult human cornea localizes to isolated fibrils, which appear randomly throughout the matrix. These studies indicate that type m collagen remains associated with collagen fibrils after removal of the amino and carboxyl propeptides, and suggests that fibrils of skin, tendon, and amnion (and presumably many other tissues that contain both types I and m collagens) are copolymers of at least types I and III collagens.T HE morphology of connective tissues is largely determined by the size and orientation of collagen fibrils. Fibril diameters vary with the tissue studied and the developmental stage of that tissue. These observations suggest that the fibril-forming process is a well controlled series of events. A number of regulatory mechanisms have been suggested. These include direct participation by cells in fibrillogenesis (Birk and Trelstad, 1986) as well as the involvement of posttranslational proteolytic processing of type I and III procollagens (Miyahara et al., 1984;Fleischmajer et al., 1985) and possibly type V collagen (Fitch et al., 1984) in the control of this process. The latter postulates are supported by the observations that types I, III, and V collagens share common structural features (Miller, 1985), and that all can form fibrils in vitro with the same periodic D-banding seen in vivo (Adachi and Hayashi, 1985).Types I, III, and V collagens all are present in haman skin at all ages but the interrelationships of these molecules are unknown. In vitro studies of fibrillogenesis have indicated the importance of helix-helix interactions in the regulation of this process (Birk and Silver, 1984). Initial studies of in vitro fibrillogenesis of mixtures of the triple-helical domains from types I and III collagens indicated that the resultant fibril diameter was inversely proportional to the I/III molar ratio (Lapiere et al., 1977). There is growing evidence that the pN-and pC-forms of both types I and HI collagens are involved in fibrillogenesis, pN-type I and pN-type III collagens are present on fibrils of small diameter, but absent from fibrils of larger diameter (Fleischmajer et al., 1981(Fleischmajer et al., , 1983(Fleischmajer et al., , 1985Sato et al., 1986). The reported persistence of the amino propeptide of pN-type I collagen in the thin and hieroglyphic fibrils of dermatosparactic animals (Lenaers et al., 1971; suggests that these globular regions further deter fiber growth or stabilization. The further observation that the amino propeptide of pN-type m collagen is excised far more slowly ...

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confidence: 65%

mentioning

confidence: 99%

Type III collagen can be present on banded collagen fibrils regardless of fibril diameter.

Keene

Sakai

Bächinger

et al. 1987

The Journal of Cell Biology

250

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“…Collagen fibril formation is a complex process that is regulated by a number of different factors, including: the collagen type or types present (2,37), the sequence and extent of propeptide processing (14,15,38), interactions with other matrix components (7,41), as well as a direct involvement of the cells (3,4,45). The collagen composition, distribution of collagen types, and fibril organization are characteristic of different connective tissues.…”

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confidence: 99%

Collagen type I and type V are present in the same fibril in the avian corneal stroma.

Birk

Fitch

Babiarz

et al. 1988

The Journal of Cell Biology

364

213

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Abstract. The distribution, supramolecular form, and arrangement of collagen types I and V in the chicken embryo corneal stroma were studied using electron microscopy, collagen type-specific monoclonal antibodies, and a preembedding immunogold method. Double-label immunoelectron microscopy with colloidal gold-tagged monoclonal antibodies was used to simultaneously localize collagen type I and type V within the chick corneal stroma. The results definitively demonstrate, for the first time, that both collagens are codistributed within the same fibril. Type I collagen was localized to striated fibrils throughout the corneal stroma homogeneously. Type V collagen could be localized only after pretreatment of the tissue to partially disrupt collagen fibril structure. After such pretreatments the type V collagen was found in regions where fibrils were partially dissociated and not in regions where fibril structure was intact. When pretreated tissues were double labeled with antibodies against types I and V collagen coupled to different size gold particles, the two collagens colocalized in areas where fibril structure was partially disrupted. Antibodies against type IV collagen were used as a control and were nonreactive with fibrils. These results indicate that collagen types I and V are assembled together within single fibrils in the corneal stroma such that the interaction of these collagen types within heterotypic fibrils masks the epitopes on the type V collagen molecule. One consequence of the formation of such heterotypic fibrils may be the regulation of corneal fibril diameter, a condition essential for corneal transparency.T HE structure of collagen fibrils, the grouping of fibrils into bundles, and the organization of fibril bundles within the stroma are all important in the determination of extracellular matrix structure and function. The corneal stroma is a highly organized connective tissue in which the rigid control of fibril diameter and the precise arrangement of the collagen fibrils is essential for optical transparency (9). Corneal collagen fibrils have a monotony of small diameter fibrils (•25 nm) with a constant center to center spacing. The fibrils are further organized into orthogonal lamellae (3, 18-20, 45, 46). This uniformity and order at all levels of matrix architecture makes the corneal stroma an ideal tissue for studies on the in situ regulation of collagen fibrillogenesis.Collagen fibril formation is a complex process that is regulated by a number of different factors, including: the collagen type or types present (2, 37), the sequence and extent of propeptide processing (14,15,38), interactions with other matrix components (7, 41), as well as a direct involvement of the cells (3,4,45). The collagen composition, distribution of collagen types, and fibril organization are characteristic of different connective tissues. The earliest corneal anlagen in the embryonic chicken is the primary stroma, an acellular orthogonal fibrillar meshwork composed of collagen types I and II, produced by the co...

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“…In its absence, procollagen intermediates still bearing the N-propeptide are secreted and incorporated into the ECM. Unlike the C-propeptide, retention of the N-propeptide does not preclude fibril formation (Hulmes et al, 1989;Miyahara et al, 1984;Miyahara et al, 1982;Romanic et al, 1992); thus, it is not surprising that collagen fibrils are formed. We also (green) and transiently transfected with mCh-ST (magenta) and an ER RUSH hook.…”

Section: Discussionmentioning

confidence: 99%

“…Prior to fibrillogenesis, the N-and C-propeptide domains of procollagen are cleaved to promote correct alignment and polymerization. Removal of the C-propeptide is particularly critical as this induces self-assembly of collagen into fibrils (Hulmes et al, 1989;Kadler et al, 1987;Kadler et al, 1990;Miyahara et al, 1984;Miyahara et al, 1982). Retention of the N-propeptide, on the other hand, does not preclude fibril assembly but can affect fibril morphology (Bornstein et al, 2002;Hulmes et al, 1989;Romanic et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Giantin is required for intracellular N-terminal processing of type I procollagen

Stevenson

Bergen

et al. 2021

Journal of Cell Biology

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Knockout of the golgin giantin leads to skeletal and craniofacial defects driven by poorly studied changes in glycosylation and extracellular matrix deposition. Here, we sought to determine how giantin impacts the production of healthy bone tissue by focusing on the main protein component of the osteoid, type I collagen. Giantin mutant zebrafish accumulate multiple spontaneous fractures in their caudal fin, suggesting their bones may be more brittle. Inducing new experimental fractures revealed defects in the mineralization of newly deposited collagen as well as diminished procollagen reporter expression in mutant fish. Analysis of a human giantin knockout cell line expressing a GFP-tagged procollagen showed that procollagen trafficking is independent of giantin. However, our data show that intracellular N-propeptide processing of pro-α1(I) is defective in the absence of giantin. These data demonstrate a conserved role for giantin in collagen biosynthesis and extracellular matrix assembly. Our work also provides evidence of a giantin-dependent pathway for intracellular procollagen processing.

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Formation of collagen fibrils by enzymic cleavage of precursors of type I collagen in vitro.

Cited by 90 publications

References 38 publications

Type III collagen can be present on banded collagen fibrils regardless of fibril diameter.

Type III collagen can be present on banded collagen fibrils regardless of fibril diameter.

Collagen type I and type V are present in the same fibril in the avian corneal stroma.

Giantin is required for intracellular N-terminal processing of type I procollagen

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