Evidence for pretranslational regulation of collagen synthesis by procollagen propeptides.

Wu, Catherine H.; Donovan, Chantal; Wu, George Y.

doi:10.1016/s0021-9258(18)67408-3

Cited by 109 publications

(16 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Both amino-and carboxy-propeptides have been shown to have feedback inhibitory effects on collagen heterotrimeric isotype. These conflicting reports may be attributed to variations in the culturing conditions or synthesis [15][16][17]. The carboxy-propeptide pre-translationally regulates collagen synthesis by internalizing and possibly to mesangial cells, which may have dedifferentiated to the extent to result in reduced ␣2(I) expression.…”

Section: Fig 4 Electron Microscopy Confirmed the Presence Of Fibrillar Collagenmentioning

confidence: 99%

Novel collagen glomerulopathy in a homotrimeric type I collagen mouse (oim)

Phillips

Pfeiffer

Luger

et al. 2002

Kidney International

View full text Add to dashboard Cite

show abstract

Section: Fig 4 Electron Microscopy Confirmed the Presence Of Fibrillar Collagenmentioning

confidence: 99%

Novel collagen glomerulopathy in a homotrimeric type I collagen mouse (oim)

Phillips

Pfeiffer

Luger

et al. 2002

Kidney International

View full text Add to dashboard Cite

show abstract

“…Recently it has been demonstrated that the purified NH2 terminal propeptide of type I collagen can inhibit the synthesis of procollagen in fibroblasts by lowering the levels of type I procollagen mRNA (66). Perhaps this region of TS has functions other than collagen binding related to regulation of gene expression.…”

Section: Amino Acid Sequence Of Thrombospondin From Cdna Clonesmentioning

confidence: 99%

Thrombospondin: a modular adhesive glycoprotein of platelets and nucleated cells.

Frazier¹

1987

The Journal of Cell Biology

191

View full text Add to dashboard Cite

Platelet adhesion to the subendothelial matrix and the subsequent aggregation of the activated platelets is a special case of intercellular adhesion that is highly regulated and for which multiple, possibly redundant adhesive systems exist. The large "adhesive glycoproteins" such as fibrinogen, von Willebrand factor, and fibronectin and their receptors, which participate in platelet adhesion and aggregation, are not unique to platelets, and probably serve analogous functions in a variety of cell types and locations. Thrombospondin (TS)/the most abundant protein of platelet alpha-granules, has been recognized as a new member of this class of adhesive glycoproteins. Whereas other adhesive glycoproteins are contained within alpha-granules and secreted upon platelet activation, they also exist in plasma at high concentrations. Hence TS is the only member of the group that is unique to alpha-granules and whose expression in quantity at sites of platelet aggregation is absolutely dependent on platelet activation.Since its discovery in 1971, TS has been thought to have a role in platelet aggregation (3,4). This suspicion has recently been confirmed by the fnding that both monoclonal (14) and polyclonal (22, 37) antibodies against platelet TS can block the secondary or secretion-dependent phase of platelet aggregation. This result in itself, however, does not speak directly to the mechanism of TS involvement in this complex process, since antibodies against fibrinogen (62), fibronectin (13), and the platelet glycoprotein IIb/IIIa (43), the receptor on platelets for fibrinogen and fibronectin, will all block platelet aggregation. Other agents that block aggregation are short peptide sequences related either to RGDS, the cellbinding sequence of fibronectin and fibrinogen (21), or to the COOH-terminal segment of the fibrinogen gamma chain (27). Both interfere with the binding of fibrinogen, fibronectin (58), and presumably yon Willebrand factor (61) to IIb/IIIa.In addition to its localization in platelets and its presumed synthesis in megakaryocytes (42), TS has been found, using immunofluorescence localization techniques, in a variety of extracellular locations in human tissues including blood vessel, muscle, skin, kidney, and glandular epithelium (64). The biosynthesis of TS has been demonstrated in a number of normal and transformed cells in culture, including endothelial, smooth muscle, and glial cells, type II pneumocytes, fibroblasts, keratinocytes, and macrophages (1,25,26,45,46,50,57,65). Furthermore, several cell lines derived from malignancies such as HT-1080 fibrosarcoma cells and the melanoma lines C32 and G361 also make TS (54,63). This widespread expression of TS and its appearance as a component of the extracellular matrix have led to the suggestion that TS might have a role analogous to that of fibronectin and laminin in cell attachment, motility, and perhaps differentiation. TS does not appear to be an obligatory attachment factor for cultured cells such as fibroblasts, smooth muscle cells, or endothelial ...

show abstract

“…In contrast, in embryonic tissues, type I and III procollagens retaining the NH 2 -propeptide have been identified (Fleischmajer et al, 1990). It has been suggested that propeptides play a role in the regulation of fibril diameter (Fleischmajer et al, 1990), and feedback regulation of collagen synthesis (Weistner et al, 1979;Horlein et al, 1981;Wu et al, 1986;Fouser et al, 1991); however, no definitive function has been proven.…”

Section: Introductionmentioning

confidence: 99%

Type IIA Procollagen Containing the Cysteine-rich Amino Propeptide Is Deposited in the Extracellular Matrix of Prechondrogenic Tissue and Binds to TGF-β1 and BMP-2

Zhu

Oganesian

Keene

et al. 1999

The Journal of Cell Biology

246

211

View full text Add to dashboard Cite

Type II procollagen is expressed as two splice forms. One form, type IIB, is synthesized by chondrocytes and is the major extracellular matrix component of cartilage. The other form, type IIA, contains an additional 69 amino acid cysteine-rich domain in the NH2-propeptide and is synthesized by chondrogenic mesenchyme and perichondrium. We have hypothesized that the additional protein domain of type IIA procollagen plays a role in chondrogenesis. The present study was designed to determine the localization of the type IIA NH2-propeptide and its function during chondrogenesis. Immunofluorescence histochemistry using antibodies to three domains of the type IIA procollagen molecule was used to localize the NH2-propeptide, fibrillar domain, and COOH-propeptides of the type IIA procollagen molecule during chondrogenesis in a developing human long bone (stage XXI). Before chondrogenesis, type IIA procollagen was synthesized by chondroprogenitor cells and deposited in the extracellular matrix. Immunoelectron microscopy revealed type IIA procollagen fibrils labeled with antibodies to NH2-propeptide at ∼70 nm interval suggesting that the NH2-propeptide remains attached to the collagen molecule in the extracellular matrix. As differentiation proceeds, the cells switch synthesis from type IIA to IIB procollagen, and the newly synthesized type IIB collagen displaces the type IIA procollagen into the interterritorial matrix. To initiate studies on the function of type IIA procollagen, binding was tested between recombinant NH2-propeptide and various growth factors known to be involved in chondrogenesis. A solid phase binding assay showed no reaction with bFGF or IGF-1, however, binding was observed with TGF-β1 and BMP-2, both known to induce endochondral bone formation. BMP-2, but not IGF-1, coimmunoprecipitated with type IIA NH2-propeptide. Recombinant type IIA NH2-propeptide and type IIA procollagen from media coimmunoprecipitated with BMP-2 while recombinant type IIB NH2-propeptide and all other forms of type II procollagens and mature collagen did not react with BMP-2. Taken together, these results suggest that the NH2-propeptide of type IIA procollagen could function in the extracellular matrix distribution of bone morphogenetic proteins in chondrogenic tissue.

show abstract

Evidence for pretranslational regulation of collagen synthesis by procollagen propeptides.

Cited by 109 publications

References 28 publications

Novel collagen glomerulopathy in a homotrimeric type I collagen mouse (oim)

Novel collagen glomerulopathy in a homotrimeric type I collagen mouse (oim)

Thrombospondin: a modular adhesive glycoprotein of platelets and nucleated cells.

Type IIA Procollagen Containing the Cysteine-rich Amino Propeptide Is Deposited in the Extracellular Matrix of Prechondrogenic Tissue and Binds to TGF-β1 and BMP-2

Contact Info

Product

Resources

About