Changing Aspects in Surgery of Diverticulitis

Ponka, Joseph L.

doi:10.1001/archsurg.1964.01320010033005

Cited by 40 publications

(45 citation statements)

References 7 publications

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“…Decreased serum levels and abnormal tissue distribution of iron in mice hemizygous for the Picalm fit1-4R mutation suggest that iron transport from the liver to other tissues is impaired (10). Because erythroid hemoglobin synthesis places particularly heavy demands on the transferrin cycle (39), decreased efficiency of AP2-dependent clathrinmediated endocytosis due to a mutational defect in the predicted recruitment and vesicular-regulation functions of Picalm in the mutant mice could have a larger impact on transferrin endocytosis and subsequent hemoglobinization than on nonhematopoietic functions, a hypothesis that can now be tested rigorously.…”

Section: Discussionmentioning

confidence: 99%

Mutations in the clathrin-assembly gene Picalm are responsible for the hematopoietic and iron metabolism abnormalities in fit1 mice

Klebig

Wall

Potter

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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Recessive N-ethyl-N-nitrosourea (ENU)-induced mutations recovered at the fitness-1 (fit1) locus in mouse chromosome 7 cause hematopoietic abnormalities, growth retardation, and shortened life span, with varying severity of the defects in different alleles. Abnormal iron distribution and metabolism and frequent scoliosis have also been associated with an allele of intermediate severity (fit1 4R ). We report that fit1 4R , as well as the most severe fit1 5R allele, are nonsense point mutations in the mouse ortholog of the human phosphatidylinositol-binding clathrin assembly protein (PICALM) gene, whose product is involved in clathrin-mediated endocytosis. A variety of leukemias and lymphomas have been associated with translocations that fuse human PICALM with the putative transcription factor gene AF10. The Picalm fit1-5R and Picalm fit1-4R mutations are splice-donor alterations resulting in transcripts that are less abundant than normal and missing exons 4 and 17, respectively. These exon deletions introduce premature termination codons predicted to truncate the proteins near the N and C termini, respectively. No mutations in the genes encoding Picalm, clathrin, or components of the adaptor protein complex 2 (AP2) have been previously described in which the suite of disorders present in the Picalm fit1 mutant mice is apparent. These mutants thus provide unique models for exploring how the endocytic function of mouse Picalm and the transport processes mediated by clathrin and the AP2 complex contribute to normal hematopoiesis, iron metabolism, and growth.

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Section: Discussionmentioning

confidence: 99%

Mutations in the clathrin-assembly gene Picalm are responsible for the hematopoietic and iron metabolism abnormalities in fit1 mice

Klebig

Wall

Potter

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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“…Uncommitted heme plays a central role in the regulation of iron uptake in various species of cells (49) and hemoglobin synthesis in developing erythroid cells (50). Within the mitochondria, heme exerts negative feedback regulation on its own synthesis at ALAS-1 and ferrochelatase (51,52).…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization of a Newly Identified Heme-binding Protein Induced during Differentiation of urine Erythroleukemia Cells

Taketani

Adachi

Kohno³

et al. 1998

Journal of Biological Chemistry

111

110

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“…Almost all organisms are able to synthesize their own heme (11), with the exception of some pathogenic bacteria and protozoa, which feed on vertebrate blood. Recently it was shown that B. microplus also acquires its heme by the degrading hemoglobin from the ingested blood (12), being the first multicellular organism shown to be unable to synthesize the protoporphyrin ring.…”

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confidence: 99%

A Heme-binding Aspartic Proteinase from the Eggs of the Hard TickBoophilus microplus

Sorgine

Logullo

Zingali

et al. 2000

Journal of Biological Chemistry

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An aspartic proteinase that binds heme with a 1:1 stoichiometry was isolated and cloned from the eggs of the cattle tick Boophilus microplus. This proteinase, herein named THAP (tick heme-binding aspartic proteinase) showed pepstatin-sensitive hydrolytic activity against several peptide and protein substrates. Although hemoglobin was a good substrate for THAP, low proteolytic activity was observed against globin devoid of the heme prosthetic group. Hydrolysis of globin by THAP increased as increasing amounts of heme were added to globin, with maximum activation at a heme-toglobin 1:1 ratio. Further additions of heme to the reaction medium inhibited proteolysis, back to a level similar to that observed against globin alone. The addition of heme did not change THAP activity toward a synthetic peptide or against ribonuclease, a non-hemeprotein substrate. The major storage protein of tick eggs, vitellin (VT), the probable physiological substrate of THAP, is a hemeprotein. Hydrolysis of VT by THAP was also inhibited by the addition of heme to the incubation media. Taken together, our results suggest that THAP uses heme bound to VT as a docking site to increase specificity and regulate VT degradation according to heme availability.

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Changing Aspects in Surgery of Diverticulitis

Cited by 40 publications

References 7 publications

Mutations in the clathrin-assembly gene Picalm are responsible for the hematopoietic and iron metabolism abnormalities in fit1 mice

Mutations in the clathrin-assembly gene Picalm are responsible for the hematopoietic and iron metabolism abnormalities in fit1 mice

Molecular Characterization of a Newly Identified Heme-binding Protein Induced during Differentiation of urine Erythroleukemia Cells

A Heme-binding Aspartic Proteinase from the Eggs of the Hard TickBoophilus microplus

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