Biomaterial Database

Dipeptidyl peptidase I of lymphocytes of the human peripheral blood. 1985

Z Lojda, and E Benesová

UI	MeSH Term	Description	Entries
D008214	Lymphocytes	White blood cells formed in the body's lymphoid tissue. The nucleus is round or ovoid with coarse, irregularly clumped chromatin while the cytoplasm is typically pale blue with azurophilic (if any) granules. Most lymphocytes can be classified as either T or B (with subpopulations of each), or NATURAL KILLER CELLS.	Lymphoid Cells,Cell, Lymphoid,Cells, Lymphoid,Lymphocyte,Lymphoid Cell
D010450	Endopeptidases	A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.	Endopeptidase,Peptide Peptidohydrolases
D001853	Bone Marrow	The soft tissue filling the cavities of bones. Bone marrow exists in two types, yellow and red. Yellow marrow is found in the large cavities of large bones and consists mostly of fat cells and a few primitive blood cells. Red marrow is a hematopoietic tissue and is the site of production of erythrocytes and granular leukocytes. Bone marrow is made up of a framework of connective tissue containing branching fibers with the frame being filled with marrow cells.	Marrow,Red Marrow,Yellow Marrow,Marrow, Bone,Marrow, Red,Marrow, Yellow
D001854	Bone Marrow Cells	Cells contained in the bone marrow including fat cells (see ADIPOCYTES); STROMAL CELLS; MEGAKARYOCYTES; and the immediate precursors of most blood cells.	Bone Marrow Cell,Cell, Bone Marrow,Cells, Bone Marrow,Marrow Cell, Bone,Marrow Cells, Bone
D004152	Dipeptidyl-Peptidases and Tripeptidyl-Peptidases	A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.	Dipeptidyl Peptidase,Dipeptidyl Peptidases,Dipeptidylpeptide Hydrolase,Tripeptidyl-Peptidase,Dipeptidylpeptide Hydrolases,Tripeptidyl-Peptidases,Dipeptidyl Peptidases and Tripeptidyl Peptidases,Hydrolase, Dipeptidylpeptide,Peptidase, Dipeptidyl,Tripeptidyl Peptidase,Tripeptidyl Peptidases,Tripeptidyl-Peptidases and Dipeptidyl-Peptidases
D006651	Histocytochemistry	Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods.	Cytochemistry
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D020789	Cathepsin C	A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.	Dipeptidyl Aminopeptidase I,Dipeptidyl Peptidase I,Dipeptidyl Transferase

Related Publications

Z Lojda, and E Benesová

[Dipeptidyl peptidase IV of peripheral blood lymphocytes in patients with primary biliary cirrhosis].

February 1993, Zeitschrift fur Gastroenterologie,

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Dipeptidyl nitriles as human dipeptidyl peptidase I inhibitors.

July 2006, Bioorganic & medicinal chemistry letters,

Z Lojda, and E Benesová

Dipeptidyl peptidase IV in human lymphocytes: molecular properties.

August 1990, Biochemical Society transactions,

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Characterization of dipeptidyl peptidase IV (CD26) from human lymphocytes.

September 1992, Clinica chimica acta; international journal of clinical chemistry,

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Reduced expression of dipeptidyl peptidase (DPP) IV in peripheral blood T lymphocytes of oral cancer patients.

October 1996, Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology,

Z Lojda, and E Benesová

Expression of dipeptidyl peptidase IV-like enzymes in human peripheral blood mononuclear cells.

January 2006, Advances in experimental medicine and biology,

Z Lojda, and E Benesová

Human dipeptidyl-peptidase I. Gene characterization, localization, and expression.

April 1997, The Journal of biological chemistry,

Z Lojda, and E Benesová

Dipeptidyl peptidase IV (CD26) on human lymphocytes. Synthetic inhibitors of and antibodies against dipeptidyl peptidase IV suppress the proliferation of pokeweed mitogen-stimulated peripheral blood mononuclear cells, and IL-2 and IL-6 production.

August 1993, Immunobiology,

Z Lojda, and E Benesová

Evolutionary Analysis of Dipeptidyl Peptidase I.

February 2022, International journal of molecular sciences,