-This-report-shows-that-all-forms-contain-substantial-peptides-which-are-resistant-to-bacterial-collagenase-and-concludes-that-type-V-collagens-differ-from-the-intestitial-collagens-types-I-II-III-in-retaining-large-noncollagenous-peptides-in-tissues-d

A peptide becomes transiently attached to the processing intermediate p alpha A by a reducible linkage. The conversion of procollagen V to p-collagen V was inhibited by colchicine and arginine. Previously, the disulfide-linked heterotrimer [(pro alpha B)2 (pro alpha A)] was found and additional procollagens containing only B type molecules were inferred. Further investigations reported here agree with these conclusions and also indicate that some trimeric molecules containing more than one chain Analysis of collagen fiber domain organization by Fourier second harmonic We present an automated and systematic two-dimensional discrete Fourier transform (2D-FFT) approach to analyze collagen fiber organization through the use of second harmonic generation (SHG) microscopy. Average orientations of individual domains and Ising-like order parameters introduced to characterize the correlation between orientations of adjacent domains may be used to quantitatively characterize fibrous tissues. Our approach was applied to analyze tissues including rat tail tendon, mouse skin, bovine corneas, and human corneas.

We also show that collagen fiber organization in normal and keratokonus human corneas may be distinguished. The current approach may be used for the quantitative differentiation of SHG collagen fiber morphology in different tissues and may be applied for diagnostic purposes.Breast cancer cells exhibit selective modulation induced by different collagen During the invasive phase of malignant tumors, neoplastic cells break into the basal lamina and enter in contact with the underlying connective tissue, which concurrently undergoes extensive modifications. The aim of our present minireview is to focus the changes in the collagenous matrix occurring during breast cancer progression and to explore the possible effects of different collagen substrates on breast cancer cell behavior and proteomic modulation.Variations in the carbohydrate content of human and bovine polymeric collagens Grant ME, Freeman IL, Schofield JD, Jackson DS.Fibronectin and the pericellular matrix of normal and transformed adherent Vaheri A, Alitalo K, Hedman K, Keski-Oja J, Kurkinen M, Wartiovaara J.Fibronectin is a major glycoprotein component of normal fibroblasts in culture.

External fibronectin is predominantly present in a pericellular fibrillar matrix that mediates distant cell-cell and cell-substratum contacts. A small proportion of external fibronectin is closely associated with the plasma membrane. In the matrix, fibronectin is partially disulfide bonded into complexes. Plasma transglutaminase, activated by thrombin, also cross-links external fibronectin into high-molecular-weight covalent complexes. In cultures of normal fibroblasts, pericellular matrix fibronectin displays extensive codistribution with (pro)collagens types I and III. Transformed adherent cells show decreased formation of the fibronectin-collagen matrix. The deficient synthesis of fibronectin and other matrix components and abnormal interactions with the matrix may account for several phenotypic characteristics of transformed cells.

collagen supplementation has been prepared by use of deoxycholate and hypotonic medium to solubilize the cells. The matrix contains glycosaminoglycans, procollagens, and fibronectin. Seebio powder collagen with the procollagens. The matrix may be considered to be an in vitro equivalent of the connective tissue matrix and basal laminae found in vivo. Human sarcoma cells spread rapidly on the prepared matrix and assume an elongated morphology characteristic of normal fibroblasts. The prepared matrix may provide a general tool to study the effects of matrix on cellular behavior and differentiation.mRNA levels for alpha-subunit of prolyl 4-hydroxylase and fibrillar collagens in University of Jyväskylä, FIN-40351 Jyväskylä, Finland.

There is evidence that immobilization causes a decrease in total collagen synthesis in skeletal muscle within a few days. In this study, early immobilization effects on the expression of prolyl 4-hydroxylase (PH) and the main fibrillar collagens at mRNA and protein levels were investigated in rat skeletal muscle. The right hindlimb was immobilized in full plantar flexion for 1, 3, and 7 days. API -state mRNAs for alpha- and beta-subunits of PH and type I and III procollagen, PH activity, and collagen content were measured in gastrocnemius and plantaris muscles. Type I and III procollagen mRNAs were also measured in soleus and tibialis anterior muscles. The mRNA level for the PH alpha-subunit decreased by 49 and 55% (P < 01) in gastrocnemius muscle and by 41 and 39% (P < 05) in plantaris muscle after immobilization for 1 and 3 days, respectively. PH activity was decreased (P < 05-01) in both muscles at days 3 and 7.

The mRNA levels for type I and III procollagen were decreased by 26-56% (P < 05-001) in soleus, tibialis anterior, and plantaris muscles at day 3. The present results thus suggest that pretranslational downregulation plays a key role in fibrillar collagen synthesis in the early phase of immobilization-induced muscle atrophy.