PMID- 24131508
OWN - NLM
STAT- MEDLINE
DCOM- 20140924
LR  - 20140210
IS  - 1475-2719 (Electronic)
IS  - 0029-6651 (Linking)
VI  - 73
IP  - 1
DP  - 2014 Feb
TI  - Food protein hydrolysates as a source of dipeptidyl peptidase IV inhibitory 
      peptides for the management of type 2 diabetes.
PG  - 34-46
LID - 10.1017/S0029665113003601 [doi]
AB  - The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is 
      estimated that by 2030 approximately 366 million people will be diagnosed with 
      this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an 
      emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous 
      aminodipeptidase that cleaves incretins such as glucagon like peptide 1 (GLP-1) 
      and glucose-dependent insulinotropic polypeptide (GIP), resulting in a loss in 
      their insulinotropic activity. Synthetic DPP-IV drug inhibitors are being used to 
      increase the half-life of the active GLP-1 and GIP. Dietary intervention is 
      accepted as a key component in the prevention and management of T2DM. Therefore, 
      identification of natural food protein-derived DPP-IV inhibitors is desirable. 
      Peptides with DPP-IV inhibitory activity have been identified in a variety of 
      food proteins. This review aims to provide an overview of food protein 
      hydrolysates as a source of the DPP-IV inhibitory peptides with particular focus 
      on milk proteins. In addition, the proposed modes of inhibition and 
      structure-activity relationship of peptide inhibitors are discussed. Milk 
      proteins and associated peptides also display insulinotropic activity and help 
      regulate blood glucose in healthy and diabetic subjects. Therefore, milk protein 
      derived peptide inhibitors may be a unique multifunctional peptide approach for 
      the management of T2DM.
FAU - Power, Orla
AU  - Power O
AD  - Department of Life Sciences, University of Limerick, Castletroy, Limerick, 
      Ireland.
FAU - Nongonierma, A B
AU  - Nongonierma AB
AD  - Department of Life Sciences, University of Limerick, Castletroy, Limerick, 
      Ireland.
FAU - Jakeman, P
AU  - Jakeman P
AD  - Food for Health Ireland, University of Limerick, Castletroy, Limerick, Ireland.
FAU - FitzGerald, R J
AU  - FitzGerald RJ
AD  - Department of Life Sciences, University of Limerick, Castletroy, Limerick, 
      Ireland.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20131017
PL  - England
TA  - Proc Nutr Soc
JT  - The Proceedings of the Nutrition Society
JID - 7505881
RN  - 0 (Blood Glucose)
RN  - 0 (Dietary Proteins)
RN  - 0 (Dipeptidyl-Peptidase IV Inhibitors)
RN  - 0 (Hypoglycemic Agents)
RN  - 0 (Milk Proteins)
RN  - 0 (Peptides)
RN  - 0 (Protein Hydrolysates)
RN  - 59392-49-3 (Gastric Inhibitory Polypeptide)
RN  - 89750-14-1 (Glucagon-Like Peptide 1)
RN  - EC 3.4.14.5 (Dipeptidyl Peptidase 4)
SB  - IM
MH  - Animals
MH  - Blood Glucose/*metabolism
MH  - Diabetes Mellitus, Type 2/blood/*diet therapy/drug therapy
MH  - Dietary Proteins/*therapeutic use
MH  - Dipeptidyl Peptidase 4/blood
MH  - Dipeptidyl-Peptidase IV Inhibitors/*therapeutic use
MH  - Gastric Inhibitory Polypeptide/blood
MH  - Glucagon-Like Peptide 1/blood
MH  - Humans
MH  - Hypoglycemic Agents/pharmacology/*therapeutic use
MH  - Milk Proteins/therapeutic use
MH  - Peptides/pharmacology/*therapeutic use
MH  - Protein Hydrolysates/pharmacology/*therapeutic use
EDAT- 2013/10/18 06:00
MHDA- 2014/09/25 06:00
CRDT- 2013/10/18 06:00
PHST- 2013/10/18 06:00 [entrez]
PHST- 2013/10/18 06:00 [pubmed]
PHST- 2014/09/25 06:00 [medline]
AID - S0029665113003601 [pii]
AID - 10.1017/S0029665113003601 [doi]
PST - ppublish
SO  - Proc Nutr Soc. 2014 Feb;73(1):34-46. doi: 10.1017/S0029665113003601. Epub 2013 
      Oct 17.