Intestinal lactase‐phlorizin hydrolase (LPH): the two catalytic sites; the role of the pancreas in pro‐LPH maturation

@article{Zecca1998IntestinalLH,
  title={Intestinal lactase‐phlorizin hydrolase (LPH): the two catalytic sites; the role of the pancreas in pro‐LPH maturation},
  author={Laura Zecca and Jos{\'e} Emilio Mesonero and Anton Stutz and J. C. Poir{\'e}e and Jean François Giudicelli and Raffaele Cursio and Sergio M. Gloor and Giorgio Semenza},
  journal={FEBS Letters},
  year={1998},
  volume={435}
}
Molecular and cellular aspects and regulation of intestinal lactase-phlorizin hydrolase
TLDR
Light is shed on important strucural and biosynthetic aspects of LPH, the role played by particular regions of the LPH protein in its transport, polarized sorting, and function, as well as on the gene expession and regulation of the activity of the enzyme.
Molecular and cellular aspects and regulation of intestinal lactase-phlorizin hydrolase.
  • H. Naim
  • Biology
    Histology and histopathology
  • 2001
TLDR
Light is shed on important strucural and biosynthetic aspects of LPH, the role played by particular regions of the LPH protein in its transport, polarized sorting, and function, as well as on the gene expession and regulation of the activity of the enzyme.
Structure, biosynthesis and regulation of lactase-phlorizin hydrolase
TLDR
It is suggested that lactase-persistence is caused by a mutation that either destructs a repressive cis-element (or a cis- Element binding a destabilising protein) or creates an enhancing cis- element interacting with activating factors which increase after weaning.
The Prosequence of Human Lactase-Phlorizin Hydrolase Modulates the Folding of the Mature Enzyme*
TLDR
Data clearly demonstrate that the proregion of pro-LPH is an intramolecular chaperone that is critically essential in facilitating the folding of the intermediate form LPHβinitial in the context of the pro- LPH polypeptide.
Processing of Human Intestinal Prolactase to an Intermediate Form by Furin or by a Furin-like Proprotein Convertase*
TLDR
Radioactive amino acid sequence analysis reveals that furin recognizes the motif R-T-P-R832, a protein convertase consensus, to generate a NH2 terminus located 36 amino acids upstream of the NH2 terminal found in vivo at Ala869.
An NSP4‐dependant mechanism by which rotavirus impairs lactase enzymatic activity in brush border of human enterocyte‐like Caco‐2 cells
TLDR
It is demonstrated conclusively that the impairment of lactase enzymatic activity at the BBM of the enterocyte‐like Caco‐2 cells observed during rotavirus infection results from an inhibitory action of the secreted non‐structural rotav virus protein NSP4.
The Diverse Forms of Lactose Intolerance and the Putative Linkage to Several Cancers
TLDR
The structural and functional features of LPH protein are focused on, and the cellular and molecular mechanism required for its maturation and trafficking is summarized, in order to determine the protective or adverse effects of milk and dairy foods on the incidence of colorectal, ovarian and prostate cancers.
A comprehensive overview of substrate specificity of glycoside hydrolases and transporters in the small intestine
TLDR
In this review, a detailed overview of the molecular structure of the substrates involved is provided as a solid base to start from and to fuel research in the area of therapeutics and diagnostics.
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References

SHOWING 1-10 OF 29 REFERENCES
A Second Enzyme Defect in Acquired Lactase Deficiency: Lack of Small‐Intestinal Phlorizin‐Hydrolase
TLDR
Adult acquired lactase deficiency is accompanied by the lack of small‐intestinal phlorizin‐hydrolase activity, an enzyme which had not been previously investigated in man, and observations point to related biological regulation mechanism(s) for the two enzymes.
Proteolytic processing of human lactase-phlorizin hydrolase is a two-step event: identification of the cleavage sites.
TLDR
Proteolytic processing of human lactase-phlorizin hydrolase in transfected COS-1, Caco-2, and MDCK cells is studied using metabolic labeling, surface immunoprecipitation, protease sensitivity assays, and microsequencing to provide unambiguous evidence of a two-step processing of the enzyme.
Maturation of human intestinal lactase-phlorizin hydrolase: generation of the brush border form of the enzyme involves at least two proteolytic cleavage steps.
TLDR
It is proposed that the initial cleavage of proLPH takes place intracellularly at a site further away from Arg868-Ala869, to generate LPH beta initial; LPHbeta is subsequently cleaved extracellularly in the gut lumen, presumably by trypsin, to mature brush border LPH (LPHbeta initial).
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