Naslov
ROLE OF AMYLIN IN PANCREATIC beta-CELL DEATH: A POTENTIAL KILLER OR JUST AN INNOCENT WITNESS?

Autori
Rumora, Lada ; Žanić Grubišić, Tihana

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Kongres Hrvatskih Biokemičara i Molekularnih Biologa uz međunarodno sudjelovanje HB2000, Program i knjiga sažetaka / Floegel, Mirna - Zagreb : Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu, 2000

Skup
Kongres Hrvatskih Biokemičara i Molekularnih Biologa uz međunarodno sudjelovanje HB2000

Mjesto i datum
Zagreb, Hrvatska, 13.10.2000. - 15.10.2000

Vrsta sudjelovanja
Pozvano predavanje

Vrsta recenzije
Domaća recenzija

Ključne riječi
pancreatic beta-cells; diabetes mellitus; amylin; cell death

Sažetak
Amylin is a 37-amino acid peptide, which is produced by pancreatic islet â-cells and co-secreted with insulin in response to nutrient stimuli. Studies have demonstrated that amylin is the key protein component of amyloid deposits found in the islets of Langerhans in almost all patients with non-insulin-dependent diabetes mellitus (NIDDM). A particular region of the peptide between positions 20 and 29, termed the amyloidogenic sequence, is thought to be responsible for amyloid fibril formation by the human peptide. The sequence of human amylin is identical in those with NIDDM and non-affected individuals, and the mechanism of amyloid deposition in diabetes remains unclear at present. Furthermore, islet amyloid formation is not found in diabetic rats, whose amylin molecule has a different amino acid sequence in this molecular region. Evidence suggests that amyloid formation may be related to hypersecretion of amylin associated with hyperglycemia acting in conjunction with other unknown factors which may enhance pancreatic fibril formation. Possible roles for amylin in the pathogenesis of diabetes have been suggested. Amylin has been implicated in insulin resistance and abnormal insulin secretion, both of which are characteristic of NIDDM. The inhibitory effects of amylin on glycogen synthesis in isolated skeletal muscles have also been reported. In addition, a number of studies have suggested that human amylin may be toxic to islet â-cells. New findings regarding the role of human amylin in â-cell death and the mechanism of its cytotoxicity will be discussed.

Izvorni jezik
Engleski

Znanstvena područja
Temeljne medicinske znanosti

POVEZANOST RADA