# BIOCHEMISTRY OF MUCOPOLYSACCHARIDES

> **NIH NIH R01** · UNIVERSITY OF MICHIGAN AT ANN ARBOR · 1990 · $203,914

## Abstract

The long term goal of this research program is the characterization of
the structures, metabolism and function of connective tissue associated
protein-carbohydrate complexes as these parameters define the remodeling
of connective tissue in development and in disease.  Lysosomal enzymes
play a key role in remodeling process(es).  The recent efforts of this
laboratory have emphasized studies concerned with the characterization
and function of two membrane-associated glycoproteins involved in the
uptake and intracellular transport of lysosomal enzymes, the so-called
phosphomannosyl receptors (PMR-1, 215 kDa; and PMR-2, 41-46 kDa).

The present research study proposes to continue and to extend these
efforts.  Primary emphasis will be placed on establishing the properties
and function(s) of the novel, low molecular weight phosphomannosyl
receptor PMR-2.  The structural features of the N-linked oligosaccharides
associated with lysosomal enzymes and the phosphomannosyl receptor(s)
will be examined in detail to define their roles in the binding of ligand
to receptor.  Ligand oriented studies will focus on 1) establishing the
positional acceptor specificity of the UDP-N-acetylglucosamine:
glycoprotein N-acetylglucosamine 1-P phosphotransferase, a key enzyme in
the synthesis of the phosphomannosyl recognition marker and 2) on
establishing the role of carbohydrates present on lysosomal aggregates in
potentiating receptor-ligand interaction and intracellular transport of
such aggregates.  Receptor oriented studies will exploit the observation
that oligosaccharides N-linked to PMR-2 participate in ligand
recognition.  The effect of oligosaccharide structure(s) and position of
N-glycosylation on the polypeptide core of the receptor in potentiating
ligand binding will be examined.  In separate studies, and as an initial
step in determining the structure of the receptor(s) in membranes,
efforts will be initiated to chemically define the nature and position of
the ligand binding sites on the polypeptide cores of PMR-1 and PMR-2.
Finally, experiments are proposed to examine the feasibility of coupling
mannose 6-P to antioxidant enzymes.  The coupled enzymes will serve as
models for the specific targeting of therapeutic agents into connective
tissue-associated cells containing phosphomannosyl receptors.

"State of the art" carbohydrate, protein and immunochemical techniques
will be utilized in the conduct of the proposed studies.

## Key facts

- **NIH application ID:** 3154702
- **Project number:** 5R01AR010531-25
- **Recipient organization:** UNIVERSITY OF MICHIGAN AT ANN ARBOR
- **SAM.gov UEI:** GNJ7BBP73WE9
- **Principal Investigator:** GEORGE W JOURDIAN
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1990
- **Award amount:** $203,914
- **Award type:** 5
- **Project period:** 1979-06-01 → 1994-05-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3154702

## Citation

> US National Institutes of Health, RePORTER application 3154702, BIOCHEMISTRY OF MUCOPOLYSACCHARIDES (5R01AR010531-25). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3154702. Licensed CC0.

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