CLINIC
Fm]SCRIPPS
l r-
| ^\D titSI ARi I I uU\L,Al l(r\
( ( ) \ 1 , \ 1 l r \ l ( . { l I ( ) N \ | ) t 1 , , \ RI \ 1 t r N t
l ( ) r , r ,\lo) J { i l t l o l l R t \ l , l \ t \ l t ( ) ; \ t )
I \ Jllll,\ (.\lltoR\i.\(r11)ll
r ) 1 , l, i l
news
Sl(rlL
) j t( , 1 9- 1I t S l I ;
For Infornation:
Andrevl Jovlers
Manager, llevls Bureau
( 6 1 9 ) 5 5 4 - 8 2 9 0 ,5 5 4 - 8 1 3 3
rOR II'II'IFDII{I'E RF,LTNSE
*100788-3
lilot for release before Ocb. 7r 1988
Scripps Clinic researchers nake key find
in blood-clottinq process
IA JOLIA, OcL. 7 -- Research InsLitute of Scripps Clinic investigators
have located the section of a blood plat,elet protein inplicat.ed in the
recognition and binding of fibrinog€nr a key process in the fornntion of
bloocl clots.
pubtished today in the journal Scierce, nay lead to the
develoSnrert of antibodies and qnthetic peptides tlnt. jrterfere wilh the
thrcnrbotic process, producing ne!,/treatrnents for stroke and heart attack.
Efforts to produce these agents are underwayat the Research Instrtlrte.
The finding,
A1so, since the protein segmenthas a similar structure to regions on
other proteins concerned with cell adhesion, it may be trrcssible to produce
antibodies and other agents to control processes in which cell adiresion
plays a role, such as inflarmmtion, tissue developnrart and the netastatic
spread of turnors.
Ttre authors of the article
were Drs. Stanley D'Souza' I'lark Ginsberg,
Stephen lam and EdrrrardP1cn, and Tinpthy Burker al-l of the Researctt
Instituter
s inmunologlz department.
(More)
Page 2
Oct. 7, 1988
#100788-3
"This is a basic finding, dnd clinical applications of this work are a
long way off rn said Ginsberg. 'Hov,rever,the potential is there."
In ttre norrml process b' which bleeding is stopped, called henrostasis'
fibrinogen binds to platelet receptors. Foll-owing this, the platelets
aggregateT forming the initial
plug that stops blood leakage.
Howeverr slznthetic peptides could block this process. l'lan-nnde
peptides mimicking the structures in platelet receptors that recognize
fibrinogen would be bound to fibrinogen - thry would competitively inhibit
the plateletes'
ability
to bind to fibrirogen.
Alsor since researchers kncr,.lthe structure of the receptor region
involved in recognizing a specific site on fibrinogen, they nny be able to
produce nonoclonal antibodies that react with tlnt
thrombus formation.
#**
site'
inhibiting