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PubMed2002

Effect of low-power laser irradiation on cell growth and procollagen synthesis of cultured fibroblasts.

BACKGROUND AND OBJECTIVES: In dentistry, low-power lasers have been used in the treatment of dentin hypersensitivity, gingivitis, periodontitis, and different forms of oral ulcers. This in vitro study focuses on the biostimulation of NIH-3T3 fibroblasts by a low-power Ga-As-pulsed laser. STUDY DESIGN/MATERIALS AND METHODS: We have studied cell growth and procollagen synthesis of cultured fibroblasts submitted to low-power laser irradiation with energy densities varying from 3 to 5 J/cm(2) over a period of 1-6 days. The light source was a 120 mW Ga-As diode laser (lambda = 904 nm). Growth curves and procollagen immunoprecipitation were obtained. RESULTS: Irradiation of 3 and 4 J/cm(2) increased the cell numbers about threefold to sixfold comparing to control cultures. However, this effect was restricted to a small range of energy densities since 5 J/cm(2) had no effect on cell growth. The energy density of 3 J/cm(2) remarkably increased cell growth, with no effect on procollagen synthesis, as demonstrated by the immunoprecipitation analysis. CONCLUSIONS: Our results showed that a particular laser irradiation stimulates fibroblast proliferation, without impairing procollagen synthesis.

3T3 Cells↗
PubMed1994

Identification of alternatively spliced variants of type II procollagen in vitreous.

Adult and foetal bovine vitreous were analyzed for the presence of unprocessed and partially processed forms of type II procollagen. Type II procollagen can exist in two alternatively spliced forms: a short form which lacks a large part of the N-propeptide due to the splicing out of exon 2 and a long form in which exon 2 is expressed and which has a full-sized N-propeptide. Both splice variants were demonstrated and analyses of type II pN-collagen demonstrated that the long form predominated, the ratio of the long form to the short form being 5:1 in foetal vitreous and 1.5:1 in adult vitreous. In foetal vitreous 35% of the type II collagen extracted was in the pN form, but there was very little unprocessed type II procollagen or type II pC-collagen. In contrast, adult vitreous extracts contained relatively less type II pN-collagen, but contained larger amounts of type II pC-collagen and unprocessed type II procollagen.

Alternative Splicing↗
PubMed1995

Antisense oligonucleotide inhibits the expression of procollagen type III gene in mouse fibroblasts.

The effects of transfection of phosphorothioate antisense oligonucleotides (ASOs) into BALB/c 3T3 mouse fibroblasts on procollagen type III production were examined. Immunohistochemistry and Western blots showed that the expression of procollagen type III decreased. Semi-quantitative reverse transcription polymerase chain reaction revealed that the expression of procollagen type III mRNA was inhibited. ASOs were effective for inhibiting procollagen type III production at the gene level, although the effect was transient.

3T3 Cells↗
PubMed1989

Molecular defects of type III procollagen in Ehlers-Danlos syndrome type IV.

Fibroblasts from most patients with Ehlers-Danlos syndrome (EDS) type IV, a disorder characterized by fragility of skin, blood vessels, and internal organs, secrete reduced amounts of type III procollagen. In 7 of 8 cell strains analyzed, we found evidence of structural defects in half of the type III procollagen chains synthesized, such as deletions or bona fide amino acid substitutions, which cause delayed formation and destabilization of the collagen triple helix and, as a consequence, reduced secretion of the molecule. The data suggest that EDS type IV is often caused by heterozygosity for mutations at the COL3A1 locus, which affect the structure of type III procollagen. The triple-helical region of the molecule, like the homologous region of type I procollagen, appears to be particularly vulnerable.

DNA↗
PubMed1995

The detection of the mRNAs of procollagen types I, II and III in human fetal fingers by in situ hybridization using digoxigenin-labelled oligonucleotide probes.

Messenger RNAs (mRNAs) encoding procollagen alpha 1 type I,alpha 1 type II and alpha 1 type III have been localized in paraffin sections of human fetal fingers using digoxigenin-labelled synthetic oligonucleotide probes. The probe-mRNA hybrids were visualized using an anti-digoxin antibody amplified with sandwich techniques. These protocols provided an excellent hybridization signal with minimal background noise. The sensitivity of the protocols was nearly equivalent to that seen when using isotopic cDNA probes. In human fetal fingers, intense hybridization signals for procollagen alpha 1 type I mRNA were detected in the osteoblasts and the fibroblasts of periosteum and perichondrium, the tenocytes of tendons, fibroblasts of ligaments, the synovial membrane and deeper layers of the dermis. In contrast, positive hybridization signals for procollagen alpha 1 type II mRNA were visualized in chondrocytes and the cambial layer of perichondrium. The signals for procollagen alpha 1 type III mRNA were detected in the fibroblasts of the dermis and perichondrium. The probes which have lower melting temperatures (Tm) could not detect the corresponding mRNAs.

Base Sequence↗
PubMed1994

Effects of experimental ureteral obstruction on platelet-derived growth factor-A and type I procollagen expression in fetal metanephric kidneys.

Complete ureteral obstruction in fetal opossum kidneys has been used as an experimental method to induce tubulointerstitial damage and interstitial fibrosis. However, the molecular events underlying extracellular matrix deposition are currently unknown. Cytokines such as platelet-derived growth factor (PDGF) are considered possible participants in these processes. In this study we used a marsupial model of ureteral obstruction to examine the expression of PDGF-A and type I procollagen mRNAs by in situ hybridization. Complete unilateral ureteral obstruction was performed in six animals at midtrimester human equivalent. Obstructed kidneys, as well as the contralateral and age-matched sham kidneys, were harvested at 1, 3, 5, 10, and 20 days post obstruction. Morphological assessment of the obstructed kidneys harvested between 1 and 5 days post obstruction showed mild tubulocystic changes, interstitial fibrosis, and inflammation compared with controls. Kidneys harvested at days 10 and 20 showed moderate tubulointerstitial damage compared with kidneys harvested after 1 and 5 days. PDGF-A mRNA signal of low abundance was detected within renal interstitial cells, urothelial cells of the pelvis, and focally within epithelial cells of immature distal convoluted tubules in non-obstructed kidneys. Type I procollagen mRNA expression was spatially co-distributed with PDGF-A-expressing interstitial cells. PDGF-A and type I procollagen signal intensities in obstructed kidneys harvested 10 and 20 days post obstruction were increased several fold compared with controls and kidneys harvested 1-5 days post obstruction. Both PDGF-A and type I procollagen mRNA increases correlated with morphological features of tubulointerstitial damage. Our results suggest that PDGF-A may participate in this form of fetal kidney damage.

Animals↗
PubMed2006

Effects of hyperbaric oxygen on gene expressions of procollagen, matrix metalloproteinase and tissue inhibitor of metalloproteinase in injured medial collateral ligament and anterior cruciate ligament.

Animal experiments were performed to investigate whether and how the administration of hyperbaric oxygen (HBO) affects gene expressions of procollagens, matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) in injured medial collateral ligament (MCL) and anterior cruciate ligament (ACL). In 64 Sprague-Dawley rats, the MCL of the left knee was lacerated at the midsubstance, and the ACL of the left knee was lacerated adjacent to the tibial insertion in another 64 rats. Of these, 32 rats with lacerated MCL and 32 rats with lacerated ACL were housed in individual cages at normal atmospheric pressure (Groups MC and AC, respectively), while the remaining 64 rats were exposed to 100% oxygen at 2.5 atmospheres absolute for 2 h for 5 days a week (Groups MH and AH, respectively). Rats were sacrificed at 3, 7, 14 and 28 days postoperatively. After macroscopic examination, bilateral MCLs were harvested from Groups MC and MH, and bilateral ACLs from Groups AC and AH. Total RNA was extracted from each specimen and gene expressions of type I and type III procollagens, MMP-2, -9 and -3, and TIMP-1 and -2 were estimated using semi-quantitative reverse transcription-polymerase chain reaction (RT-PCR). Macroscopically, lacerated MCL healed by scar tissue formation, the amount of which appeared to be greater in Group MH than in Group MC. In contrast, no lacerated ACLs united, and little, if any, differences were apparent in macroscopic findings between Groups AH and AC. Gene expression of type I procollagen was significantly greater in Group MH than in Group MC at 7 days postoperatively and was also significantly greater in Group AH than in Group AC at 28 days (P<0.05). No significant differences in type III procollagen gene expression were noted between Groups MH and MC or between Groups AH and AC. In addition, no significant differences in gene expressions of MMPs were seen in either ligament, except that gene expression of MMP-13 was significantly lower at 7 days in Group MH than in Group MC (P<0.05). Gene expressions of TIMPs did not differ significantly between Groups MH and MC in each time interval, whereas gene expressions of TIMPs were significantly greater in Group AH than in Group AC at 7, 14 and 28 days for TIMP-1 and at 3, 7 and 14 days for TIMP-2 (P<0.05). RT-PCR results suggested that HBO enhances structural protein synthesis and inhibits degradative processes by enhancing TIMP activities in the lacerated ACL. However, none of the lacerated ACLs united macroscopically despite administration of HBO, indicating that the effect of HBO is insufficient for healing of the injured ACL. If HBO therapy is used as an adjunctive therapy after primary repair of the injured ACL, the success rate of surgery seems likely to be increased.

Animals↗
PubMed2003

Regulation of heat shock protein 47 and type I procollagen expression in avian tendon cells.

Heat shock protein 47 (Hsp47) is a collagen-binding stress protein that acts as a collagen-specific molecular chaperone during the biosynthesis and secretion of procollagen. Type I collagen is a major component of tendons. Coexpression of genes for both proteins has been reported in various tissues, where many growth factors likely regulate their expressions in different ways. Here we describe the effects of increased temperature, mechanical stress and growth factors on Hsp47 and type I procollagen expression in embryonic chicken tendon cells. The expression of Hsp47 mRNA at 45 degrees C increased within 60 min and returned to baseline in 4 h after the temperature decreased to 37 degrees C. Our data also show that transforming growth factor beta1 (TGF-beta1) is another regulator of Hsp47 expression as the addition of TGF-beta1 led to a moderate increase in the expression of Hsp47 mRNA. TGF-beta2 and TGF-beta3 exerted only a small effect; epidermal growth factor and tumor necrosis factor alpha (TNF-alpha) had none. TGF-beta1 increased type I procollagen mRNA expression and TNF-alpha reduced this expression. TGF-beta1 delayed the degradation of Hsp47 mRNA after heat shock likely via post-transcriptional regulation of the Hsp47 gene. We also report that mechanical stress increased Hsp47 mRNA expression and Hsp47 protein synthesis. Induction of Hsp47 protein expression by heat shock, mechanical stress and TGF-beta1 was likely achieved through activation and translocation of heat shock transcription factor 1 into the nucleus. Our data indicate that TGF-beta1 is a major regulator of both procollagen and Hsp47 genes.

Active Transport, Cell Nucleus↗
PubMed1990

Collagen metabolism in gynecologic patients: changes in the concentration of the aminoterminal propeptide of type III procollagen in serum.

We have previously found the serum concentration of the aminoterminal propeptide of type III procollagen, an indicator of collagen metabolism, to be increased in advanced ovarian cancer. In this study we measured the serum aminoterminal propeptide of type III procollagen concentration in healthy women during the menstrual cycle and in patients with salpingo-oophoritis, leiomyomas, endometriosis, and benign ovarian tumors. The concentration was higher in the luteal phase than that in the follicular phase, suggesting an association of collagen metabolism with ovarian steroid hormones. Severe salpingo-oophoritis increased the serum level of the aminoterminal propeptide of type III procollagen with a decrease to normal during recovery. Elevated values were occasionally seen in endometriosis and leiomyomas. These findings indicate that the aminoterminal propeptide of type III procollagen is a relatively unspecific indicator of ovarian carcinoma.

Adult↗
PubMed1978

The synthesis of presumptive procollagen messenger ribonucleic acid in the calvaria of the developing chick embryo.

The presumptive messenger RNAs for type I procollagen were isolated from chick embryo calvaria at various stages of development. Poly(A)-containing RNA fractions from denaturing sucrose gradients directed protein synthesis in a cell-free system derived from wheat germ. Procollagen mRNA activity was detected in a region of about 26 S. Approx. 80% of the labeled proline incorporated into cell-free product was susceptible to digestion by purified bacterial collagenase. The synthesis of procollagen mRNAs was followed during development. Comparison of the in vitro labeled mRNAs from calvaria of day 12--16 embryos indicated that the 26 S component was most pronounced at day 13 and decreased progressively towards day 16. In addition, incubation of calvaria with tritiated nucleosides for 1.5--25 h revealed that 26 S mRNA was significantly labeled only after prolonged periods. The results suggest that procollagen mRNA is a relatively stable species with a prolonged half-life compared to the majority of mRNAs in this tissue.

Animals↗
PubMed1984

Demethylation of the type I procollagen genes in transformed fibroblasts treated with 5-azacytidine.

Transformation of the human embryonic lung fibroblast line, WI-38, with simian virus 40 (SV40) results in inactivation of the type I procollagen genes. No type I collagen or procollagen mRNA is detected in these transformed cells, as determined by polyacrylamide gel electrophoresis. Analysis of the methylation patterns of these genes showed the type I procollagen genes to be hypermethylated at certain cytosine residues in the transformed cells. However, several of the cytosine residues were methylated in the normal cells where these genes are expressed. These methylation patterns can be altered by treatment of the cells with 5-azacytidine or 5-azadeoxycytidine, but without a resultant activation of the type I procollagen genes. These results show that demethylation alone is not sufficient for gene activation, but that other signals are also required.

Azacitidine↗
PubMed1991

Predominance of type III over type I cell surface procollagens in rat lung fibroblasts.

Binding assays of 125I-labeled affinity-purified monospecific type I and III procollagen antibodies to fibroblasts have revealed the presence of type I and III procollagens on the cell surface, and that the amount of type III procollagen is 10 times greater than that of type I procollagen. Analyses by flow cytometry and fluorescent microscopy after treatment with an isothiocyanate (FITC)-conjugated second antibody supported this finding.

Animals↗
PubMed1985

Quantitation of type II procollagen mRNA levels during chick limb cartilage differentiation.

A single-stranded DNA probe complementary to chicken type II procollagen mRNA has been used to quantitate levels of that mRNA present in chicken limb mesenchyme during cartilage differentiation. Excess labeled probe prepared from a cDNA template cloned in M13mp9 was hybridized to completion to increasing amounts of total RNA and assayed by protection from S1 nuclease digestion. Estimates of the absolute levels of type II procollagen RNA were determined using the M13mp9 template containing the coding strand as a standard. RNA complementary to the probe increased from 20 copies per diploid genome in stage 24 limb to approximately 2000 copies per diploid genome in stage 24 limb mesenchyme which had differentiated to cartilage in culture. Similar levels were found in cartilage from stage 31 limb. Sternal cartilage from 17-day embryos contained approximately 10,000 copies per diploid genome suggesting that the level of expression of this gene is different in limb growth cartilage compared with sternal cartilage. Low but detectable levels of RNA complementary to the probe were observed in limb at stages 20-24. Since a large fraction of the type II procollagen RNA in these early limbs is associated with polysomes, the type II procollagen gene appears to be expressed at a low level prior to phenotypic differentiation and prior to the accumulation of immunologically detectable levels of type II collagen.

Animals↗
PubMed1984

Release of amino-terminal procollagen peptides in paraquat-induced acute pulmonary fibrosis.

Acute pulmonary fibrosis following intoxication with paraquat is characterized by increased collagen synthesis and deposition in the lungs. In the present study, a chronic lung lymph fistula preparation in sheep was used to investigate the changes in procollagen type III peptide level in the lung lymph in acute pulmonary distress associated with paraquat application. The procollagen type III peptide is supposed to be an indicator of the changing biosynthetic pattern of pulmonary collagen in lung fibrosis. All animals tested showed a progressive pulmonary distress following the application of paraquat characterized by increasing lymph flows and lymph protein flows which monitored the microvascular membrane damage. In parallel to these findings, procollagen peptide levels in the lymph fluid increased, even before manifest biochemically or histologically detectable pulmonary fibrosis occurred. The present results suggest that the release of procollagen type III peptides into lymph fluid is an early indicator of beginning fibrotic tissue disarrangement, even before completed pulmonary fibrosis can be detected by common tissue analysis.

Acute Disease↗
PubMed1987

COOH-terminal propeptides of the major human procollagens. Structural, functional and genetic comparisons.

The sequences of the carboxy-terminal extensions (COOH-propeptides) of at least one chain of all of the major human procollagens have only recently been deduced, and include those of the interstitial (alpha 1(I), alpha 2(I), alpha 1(II), alpha 1(III)), basement membrane (alpha 1(IV)) and pericellular (alpha 2(V)) procollagens. Comparisons of DNA and protein sequences, corresponding to these COOH-propeptides domains, established the early divergence of the basement membrane alpha 1(IV) COOH-propeptide from the corresponding sequences of the interstitial and pericellular procollagens. The latter are relatively highly conserved and share 58% primary peptide sequence similarities, whereas sequence similarities relative to alpha 1(IV) are limited. Hydropathy profiles and secondary structure potentials further emphasize the clustering of conserved and variable regions among the interstitial and pericellular COOH-propeptides, and provided further evidence for significant structural differences between these sequences and the alpha 1(IV) COOH-propeptide. The most highly conserved sequences of the alpha 1(I), alpha 2(I), alpha 1(II), alpha 1(III) and alpha 2(V) COOH-propeptides include regions surrounding the carbohydrate attachment site, cysteine-containing regions and the COOH-terminal sequences. Cysteinyl, tyrosyl and tryptophanyl residues were found to be highly conserved as were most charged residues. Localization of variable regions, in general, occurs within hydrophilic sequences with high beta-turn potentials that are proximal to intron/exon splice junctions. The most variable sequences are associated with the telopeptides and adjoining NH2-terminal portions of the COOH-propeptides as demonstrated by predictive secondary structure analyses. These results, combined with similar analyses of abnormal alpha 2(I) COOH-propeptide (osteogenesis imperfecta) permitted the identification of subsequences that are likely to be a prerequisite for COOH-propeptide functions, namely procollagen chain recognition and nucleation sites for triple helix formation. These functions are also common to the alpha 1(IV) COOH-propeptide; however, the lack of cleavage of this region and its additional postulated structural role in extracellular matrix interactions likely account for its divergent primary and secondary structure.

Amino Acid Sequence↗
PubMed1991

Morphology of sheet-like assemblies of pN-collagen, pC-collagen and procollagen studied by scanning transmission electron microscopy mass measurements.

At high concentrations, type I pN-collagen, pC-collagen and procollagen (the first 2 generated from procollagen by enzymic cleavage of C-propeptides and N-propeptides, respectively) can all be made to assemble in vitro into thin D-periodic sheets or tapes. Scanning transmission electron microscopy mass measurements show that the pN-collagen sheets and procollagen tapes have a mass per unit area corresponding to that of approximately 6.8 monolayers of close-packed molecules. pN-collagen sheets are extensive and remarkably uniform in mass thickness (fractional S.D. 0.035); procollagen tapes are neither as extensive nor as uniform in thickness. The mean thickness of pC-collagen tapes is less and the variability is greater. In pN-collagen sheets, the overlap: gap mass contrast in a D-period is increased from 5:4 (the ratio in a native collagen fibril) to 6:4, showing that the N-propeptides do not project into the gap but are folded back over the overlap zone. Assuming all N-propeptides to be constrained to the two surfaces of a sheet, their surface density can be found from the mass thickness of the sheet. In a lateral direction (i.e. normal to the axial direction where the spacing is D-periodic), the N-propeptide domains are calculated to be spaced, centre to centre, by 2.23 (+/- 0.1) nm on both surfaces. This value (approx. 1.5 x the triple-helix diameter) implies close-packing laterally with adjacent domains in contact. Sheet formation and the "surface-seeking" behaviour of propeptides can be understood in terms of the dual character of the molecules, evident from solubility data, with propeptides possessing interaction properties very different from those displayed by the rest of the molecule. The form and stability of sheets (and of first-formed fibrils assembling in vivo) could, it is suggested, depend on the partially fluid-like nature of lateral contacts between collagen molecules.

Animals↗
PubMed1991

Serum type I collagen and N-terminal peptide of type III procollagen in chronic hepatitis. Relationship to liver histology and conventional liver tests.

The aim of this study was to compare serum N-terminal peptide of type III procollagen to aminotransferases and gamma-globulins as a marker for histological activity in patients with chronic hepatitis and to assess the role of type I collagen, a new serum marker, as a marker of fibrosis in these patients. Sixty patients with biopsy-proven chronic hepatitis were included in this study. Liver disease was virus B-related in 29, autoimmune in five, drug-induced in five, and of unknown etiology in 21. Each biopsy was independently assessed by two liver pathologists. Two histological scores, a score of activity and a score of fibrosis, were established. Serum N-terminal peptide of type III procollagen and type I collagen were assayed by liquid phase RIA. Significant correlations were noted between serum N-terminal peptide of type III procollagen and scores of activity (r = 0.70, p less than 10(-4)) and fibrosis (r = 0.45, p = 0.0005), and between serum type I collagen and scores of activity (r = 0.46, p = 0.0004) and fibrosis (r = 0.67, p less than 10(-4)). When the correlation between scores of activity and fibrosis (r = 0.52, p = 10(-4)) was considered by partial correlation, serum N-terminal peptide of type III procollagen was correlated with the score of activity (r = 0.63, p less than 10(-3)) but not with the score of fibrosis, and serum type I collagen was correlated with the score of fibrosis (r = 0.58, p less than 10(-3)), but not with the score of activity.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1999

Reproductive hormones and aminoterminal propeptide of type III procollagen in serum as early markers of pelvic pain during late pregnancy.

OBJECTIVE: The object was to study serum concentrations of reproductive hormones and aminoterminal propeptide of type III procollagen in early pregnancy as markers of pelvic pain (sacral pain or symphyseal pain) during later pregnancy. STUDY DESIGN: A prospective, clinical cohort study was performed, with repeated examinations of 200 women. RESULTS: Serum concentrations of relaxin and serum concentrations of propeptide of type III procollagen (a collagen turnover marker) measured in early pregnancy were significantly correlated with pelvic pain with onset during pregnancy and reported in late pregnancy (positively and negatively, respectively). In a multivariate analysis, relaxin and propeptide of type III procollagen concentrations remained independently and significantly correlated with pelvic pain. CONCLUSION: Serum concentrations of relaxin and propeptide of type III procollagen measured in early pregnancy may reflect the cause of and indicate an increased risk of pelvic pain (back pain or symphyseal pain) during late pregnancy. The mechanism is unclear.

Adolescent↗