Serum and Urine Analysis of the Aminoterminal Procollagen Peptide Type III by Radioimmunoassay with Antibody Fab Fragments

Rohde, Heilwig; Langer, I.; Krieg, Thomas; Timpl, Rupert

doi:10.1016/s0174-173x(83)80018-1

Cited by 66 publications

(35 citation statements)

References 15 publications

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“…Therefore, assays that also measure the degraded forms (e.g. Col 1) were developed (16,19). The average ratio between Col 1-3 propeptide concentration and the Col 1 fragment determined by molecular sieve chromatography is about 1:4 in the serum of adults.…”

Section: Discussionmentioning

confidence: 99%

“…Finally, from the data of Rhode e t al. (16) and the study of Keller et al (22), it was presumed that measurement of the PIIINP level in amniotic fluid by the conventional PIIINP RIA would be of low precision and sensitivity, because it was anticipated that mainly propeptide fragments would be present if originating from fetal urine (the major constituent of amniotic fluid in the late-gestation fetus), inasmuch as in adults proteolytic degradation apparently must precede the urinary excretion of the propeptide (16). However, recent data from Danne e t al.…”

Section: Discussionmentioning

confidence: 99%

“…PIIINP concentration was measured in duplicate by a research version of the PIIINP assay (16). Monovalent Fab' antibody fragments are used instead of the antiserum (Behringwerke AG, Marburg, Germany).…”

Section: Methodsmentioning

confidence: 99%

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Aminoterminal Propeptide of Type III Procollagen in Cord Blood and Amniotic Fluid of Appropriate-for-Gestational-Age Infants: A Predictor of Age-Related Fetal Growth Rate

et al. 1994

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Procollagen propeptide serum levels reflect the rate of collagen production. Because the prenatal period is unrivaled in terms of relative amounts of collagen synthesized per unit of time, this life episode must be the most sensitive period for the study of these biochemical markers of growth variability. N-terminal propeptide of type 111 procollagen (PIIINP) concentration was measured by two different methods (Fabl-fragment and whole antibodybased RIA assay) on paired samples of cord serum and amniotic fluid from a study cohort of 602 perinates with gestational age ranging from 20 to 41 wk. The aim of this study is to assess the clinical usefulness of the PIIINP assay for the evaluation of fetal somatic growth variation during the second half of normal pregnancies. It was demonstrated that the PIIINP level in cord serum, as well as in amniotic fluid, reflects age-related growth activity in "healthy" fetuses (n = 504) with normal intrauterine growth. This reflection was independent of the cumulative body mass or length Because collagen is the main structural component of connective tissue, its generation must be a prerequisite for somatic growth (1). Earlier findings indicated a close relation between urinary excretion of hydroxyproline (a major amino acid constituent of collagen molecules) and growth rate throughout childhood (2).Collagen type 111, the most abundant protein in the extracellular matrix, is synthesized in the cell as procollagen I11 (1). After its secretion, the aminoterminal and carboxyterminal propeptides are cleaved off by specific peptidases and released into the serum (3). Their amount is in a stoichiometric relationship to the number of col-

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Aminoterminal Propeptide of Type III Procollagen in Cord Blood and Amniotic Fluid of Appropriate-for-Gestational-Age Infants: A Predictor of Age-Related Fetal Growth Rate

et al. 1994

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“…Elevated serum PIIINP may reflect enhanced synthesis and deposition of fibrillar collagen or alteration in degradation and elimination of circulating PIIINP.1" Within recent years, radioimmunoassays detecting PIIINP-related antigens have been developed. [12][13][14] assays differ with respect to the antigen forms preferentially measured in serum.…”

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confidence: 99%

Serum aminoterminal type III procollagen peptide reflects repair after acute myocardial infarction.

et al. 1990

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“…Radioimmunoassays based on antibodies measure mainly the intact form of aminopropeptide. Recent studies using Fab' fragments [33] have shown that such assays are more versatile and allow the quantitative analysis of the total amount of aminopropeptide including its fragments in serum and urine. This will be of value in many biological and clinical studies.…”

Section: Discussionmentioning

confidence: 99%

Immunochemical properties of the aminopropeptide of procollagen type III

Rohde¹,

Brückner²,

Timpl

1983

Eur J Biochem

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The precursor-specific aminopropeptide of bovine type 111 procollagen is a strong immunogen in rabbits, guinea pigs and mice and induces antibodics which do not cross-react with type I procollagen. The antibody response is regulated by immune response genes associated with the major histocompatibility complex. Major antigenic determinants were found in the compact, non-collagenous domain (fragment Col 1) located at the N terminus of the aminopropeptide and were destroyed by reduction ofdisulfide bonds. Minor antigenic determinants independent of disulfide bonds also exist in fragment Col 1 and could be localized on a distinct tryptic peptide. Fragment Col 1 showed a lower affinity for antibody when compared with the intact aminopropeptide which causes a non-parallel shift in radioimmuno-inhibition profiles. Monovalent antibody fragments showed an average tenfold reduction in affinity constant and failed to distinguish bctween aminopropeptide and fragment Col 1. This indicates that the stronger binding of bivalent antibody by the triple-stranded aminopropeptide is due to multiple interactions with both antibody binding sites which are lost for a single-stranded antigen (Col 1) or with monovalent antibody fragments.Aminopropeptides are precursor-specific segments located at the amino end of procollagens. They are liberated during the conversion of the precursor into collagen [1,2] and are considered to play important roles in regulating collagen synthesis [3] and fibril formation [4,5]. The amino acid sequence of the aminopropeptides of procollagen I and 111 has been elucidated [2,6,7] supporting previous evidence on three structurally and conformationally distinct domains [8 -101 in each peptide segment. Specific antibodies could be raised against both types of aminopropeptide [9,11] and were useful tools in several structural and biological studies [4,12 -141. It was also found that the antibody response in mice to the aminopropeptide of procollagen I is under H-2 linked genetic control [I 51. lmmunochemical studics with the procollagen I aminopropeptide [13,16] indicated that only certain structures are antigenically important. Similar data are still lacking for the homologous segment of procollagen 111. However, antibodies against this peptide have been of value for studying its matrix function [4] and for developing sensitive radioimmunoassays for quantifying circulating antigens under clinical conditions [I 71. The latter approach indicated different affinities for the intact aminopropeptide and smaller antigenic fra'gments which may arise in the body due to physiologic dcgradation [I 7 -191. In the present study we have tried to explore the structural basis for these observations. A h h i w i u r m . pN-collagen rcfers to a partially processed form of procollagen which has lost its carboxypropeptide but still possesses its aminopropeptide.

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Serum and Urine Analysis of the Aminoterminal Procollagen Peptide Type III by Radioimmunoassay with Antibody Fab Fragments

Cited by 66 publications

References 15 publications

Aminoterminal Propeptide of Type III Procollagen in Cord Blood and Amniotic Fluid of Appropriate-for-Gestational-Age Infants: A Predictor of Age-Related Fetal Growth Rate

Aminoterminal Propeptide of Type III Procollagen in Cord Blood and Amniotic Fluid of Appropriate-for-Gestational-Age Infants: A Predictor of Age-Related Fetal Growth Rate

Serum aminoterminal type III procollagen peptide reflects repair after acute myocardial infarction.

Immunochemical properties of the aminopropeptide of procollagen type III

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