# BIOSYNTHESIS OF PROLYL HYDROXYLASE

> **NIH NIH R01** · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · 1988 · $168,635

## Abstract

This study aims at describing the role of lysosomes in regulating collagen
production in fibroblasts.  The regulation of collagen has clear
health-related implications because of the number of human diseases that
are associated with a change in collagen metabolism.  Acquired disorders
such as rheumatoid arthritis, pulmonary fibrosis, cirrhosis, and
atherosclerosis, involve significant changes in collagen content and type
in affected tissues.  The genetic disorders such as the Ehlers Danlos
syndromes and Osteogenesis Imperfecta demonstrate various aspects of
deficiencies in collagen regulation.  Based on recent data from several
laboratories that intracellular degradation of newly synthesized collagen
is widespread in fibroblasts and that it can in part be inhibited by
lysosomal inhibitors, a role for lysosomes in collagen biosynthesis has
been implicated.  One role of lysosomes has been shown to involve the
degradation, intracellularly, of a portion of newly synthesized,
structurally defective, collagen.  A second role for lysosomes to be tested
here is their hypothesized involvement in the translational regulation of
collagen synthesis and its secretion.  The role of lysosomes is, however,
complicated by the presence of at least one non-lysosomal pathway for the
basal levels of intracellular degradation of newly synthesized collagen.
The first aim of the present proposal is to use cultured chick tendon
fibroblasts to determine if procollagen or procollagen fragments are found
in lysosomes.  The second aim is to examine cultured fibroblasts which are
inhibited in theri ability to secrete procollagen to determine if decreased
secretion also results in decreased translation, and if this decreased
translation is a result of regulation of procollagen production involving
lysosomes.  The third aim is to determine whether lysosomes may be involved
in the uptake of either procollagen or procollagen extension propeptides
either alone or by a receptor-mediated process.  In order to characterize
further intracellular degradation in cultured fibroblasts, the fourth aim
is to examine the basal level of degradation to determine if oxygen-derived
free radicals and/or neutral proteases are responsible for this important
non-lysosomal pathway.

## Key facts

- **NIH application ID:** 3156116
- **Project number:** 5R01AR031839-05
- **Recipient organization:** UNIV OF MED/DENT NJ-R W JOHNSON MED SCH
- **Principal Investigator:** RICHARD A BERG
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1988
- **Award amount:** $168,635
- **Award type:** 5
- **Project period:** 1983-04-01 → 1988-11-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3156116

## Citation

> US National Institutes of Health, RePORTER application 3156116, BIOSYNTHESIS OF PROLYL HYDROXYLASE (5R01AR031839-05). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3156116. Licensed CC0.

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