# PROCOLLAGEN: SECRETION, ASSEMBLY AND CELL RECEPTORS

> **NIH NIH R01** · UNIVERSITY OF WISCONSIN-MADISON · 1989 · $146,146

## Abstract

The general aim of the proposal is to define the mechanisms that govern the
secretion of procollagen and its conversion to fibrillar forms in the
extracellular matrix.  Such knowledge is critical for an understanding of
matrix-cell interactions in the course of embryonic differentiation and
tissue repair after injury.  The major hypotheses of the proposal are:  1)
that native, soluble type I procollagen is bound at the fibroblast surface
in the course of its secretion; 2) that the procollagen binds to a unique
receptor that may also function in the transcellular transport of
procollagen; and 3) that surface binding of procollagen is determinate for
fibrillogenesis and required for incorporation of procollagen into fibrils
in the extracellular matrix (ECM).  Experiments include:  1) ruling out
fibronectin or fibronectin cell receptors as determinants of procollagen
binding; 2) following the movement of added 125I-procollagen ligand and
metabolically-labeled procollagen from cell surface to insoluble ECM in
short (0-3 hr.) and long (0-25 hr.) labeling and chase experiments; 3)
assessing the role of disulfide multimer assembly for incorporation of
procollagen into the ECM; 4) identifying the intermediates of procollagen
processing that are cell-surface bound and that are incorporated into the
ECM; 5) characterizing the procollagen receptor protein(s) in the plasma,
smooth and ERR membranes by means of nitrocellulose filter binding assays,
affinity chromatography, PAGE, western blotting with 125I-procollagen as
the probe, and labeling the receptor(s) with photoaffinity cross-linkers;
6) developing polyclonal and monoclonal antibodies to the receptor(s) and
employing them in the studies of receptor structure, function, localization
and metabolism; and 7) using gold-labeled antibodies to procollagen to
visualize at the ultrastructural level specific binding of exogenously
added procollagen to the fibroblast surface.

## Key facts

- **NIH application ID:** 3158451
- **Project number:** 5R01AR038174-03
- **Recipient organization:** UNIVERSITY OF WISCONSIN-MADISON
- **SAM.gov UEI:** LCLSJAGTNZQ7
- **Principal Investigator:** BURT D GOLDBERG
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1989
- **Award amount:** $146,146
- **Award type:** 5
- **Project period:** 1986-12-01 → 1991-11-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3158451

## Citation

> US National Institutes of Health, RePORTER application 3158451, PROCOLLAGEN: SECRETION, ASSEMBLY AND CELL RECEPTORS (5R01AR038174-03). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3158451. Licensed CC0.

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