PMID- 35455074
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20220716
IS  - 2075-1729 (Print)
IS  - 2075-1729 (Electronic)
IS  - 2075-1729 (Linking)
VI  - 12
IP  - 4
DP  - 2022 Apr 14
TI  - Factors That Contribute to hIAPP Amyloidosis in Type 2 Diabetes Mellitus.
LID - 10.3390/life12040583 [doi]
LID - 583
AB  - Cases of Type 2 Diabetes Mellitus (T2DM) are increasing at an alarming rate due 
      to the rise in obesity, sedentary lifestyles, glucose-rich diets and other 
      factors. Numerous studies have increasingly illustrated the pivotal role that 
      human islet amyloid polypeptide (hIAPP) plays in the pathology of T2DM through 
      damage and subsequent loss of pancreatic beta-cell mass. HIAPP can misfold and form 
      amyloid fibrils which are preceded by pre-fibrillar oligomers and monomers, all 
      of which have been linked, to a certain extent, to beta-cell cytotoxicity through a 
      range of proposed mechanisms. This review provides an up-to-date summary of 
      recent progress in the field, highlighting factors that contribute to hIAPP 
      misfolding and aggregation such as hIAPP protein concentration, cell stress, 
      molecular chaperones, the immune system response and cross-seeding with other 
      amyloidogenic proteins. Understanding the structure of hIAPP and how these 
      factors affect amyloid formation will help us better understand how hIAPP 
      misfolds and aggregates and, importantly, help identify potential therapeutic 
      targets for inhibiting amyloidosis so alternate and more effective treatments for 
      T2DM can be developed.
FAU - Sevcuka, Adriana
AU  - Sevcuka A
AD  - Molecular Systems for Health Research Group, School of Human Sciences, London 
      Metropolitan University, London N7 8DB, UK.
FAU - White, Kenneth
AU  - White K
AUID- ORCID: 0000-0002-6103-9078
AD  - Molecular Systems for Health Research Group, School of Human Sciences, London 
      Metropolitan University, London N7 8DB, UK.
FAU - Terry, Cassandra
AU  - Terry C
AUID- ORCID: 0000-0002-8611-8821
AD  - Molecular Systems for Health Research Group, School of Human Sciences, London 
      Metropolitan University, London N7 8DB, UK.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20220414
PL  - Switzerland
TA  - Life (Basel)
JT  - Life (Basel, Switzerland)
JID - 101580444
PMC - PMC9025880
OTO - NOTNLM
OT  - aggregation
OT  - amyloidosis
OT  - human islet amyloid polypeptide
OT  - type 2 diabetes mellitus
COIS- The authors declare no conflict of interest.
EDAT- 2022/04/24 06:00
MHDA- 2022/04/24 06:01
PMCR- 2022/04/14
CRDT- 2022/04/23 01:05
PHST- 2022/03/21 00:00 [received]
PHST- 2022/04/01 00:00 [revised]
PHST- 2022/04/12 00:00 [accepted]
PHST- 2022/04/23 01:05 [entrez]
PHST- 2022/04/24 06:00 [pubmed]
PHST- 2022/04/24 06:01 [medline]
PHST- 2022/04/14 00:00 [pmc-release]
AID - life12040583 [pii]
AID - life-12-00583 [pii]
AID - 10.3390/life12040583 [doi]
PST - epublish
SO  - Life (Basel). 2022 Apr 14;12(4):583. doi: 10.3390/life12040583.