# BIOCHEMICAL, STRUCTURAL STUDIES OF KININ-FORMING SYSTEMS

> **NIH NIH R01** · STATE UNIVERSITY OF NEW YORK AT BUFFALO · 1987 · $101,035

## Abstract

The objective of this research is to characterize the biochemical and
structural features of the components of kinin-forming systems in rodent
plasma and both normal and neoplastic tissue.  The components to be studied
include both alkaline (kallikrein) and acid kinin-forming proteases,
kininogen substrates, vasoactive peptides formed by the interaction of
respective proteases and kininiogen substrates and kinin-destroying
(kininase) enzymes.  This long-term objective will be achieved by studying
the detailed physical-chemical and structural aspects of each molecular
species as well as the protein-protein interactions.  The study of the role
of the carbohydrates in the function of such glycoprotein components as
kallikrein and kininogen will be a central specific aim of this research.
Carbohydrate moieties of glycoproteins have been shown to be functionally
involved in protein aggregation or oligomerization similar to that observed
with rat plasma kininogen.  These moieties from glycoprotein components
derived from different tissue sources including neoplastic and blood will
be compared and their structure-function (esterolytic and kinin-forming)
relationships studied.  In view of the involvement of the kinin-forming
systems in a wide variety of physiological and pathologic conditions,
clarification of molecular factors influencing kinin formation may
contribute to our understanding and possibly control of the respective
process.  This research also proposes to study the cellular site of
localization and biosynthesis of major components of the kinin-forming
system.  Immunohistochemical and tissue perfusion with tritiated amino
acids technique will be utilized.  The component molecular species derived
from the perfusion studies will be compared with system components purified
from normal and malignant tissue and blood.  Knowledge of the site(s) of
synthesis of the kinin-forming enzymes and substrates should help us define
more precisely the role of the kinin-forming systems in health and disease

## Key facts

- **NIH application ID:** 3176356
- **Project number:** 5R01CA038270-02
- **Recipient organization:** STATE UNIVERSITY OF NEW YORK AT BUFFALO
- **SAM.gov UEI:** LMCJKRFW5R81
- **Principal Investigator:** NATHAN BACK
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $101,035
- **Award type:** 5
- **Project period:** 1986-08-01 → 1989-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3176356

## Citation

> US National Institutes of Health, RePORTER application 3176356, BIOCHEMICAL, STRUCTURAL STUDIES OF KININ-FORMING SYSTEMS (5R01CA038270-02). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3176356. Licensed CC0.

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