Disease relevance of LECT2

• In addition, several human hepatoma cell lines also expressed LECT2 mRNA, suggesting that hepatic cells in the liver produce LECT2 protein [1].

High impact information on LECT2

• p33, an endogenous target protein for arginine-specific ADP-ribosyltransferase in chicken polymorphonuclear leukocytes, is highly homologous to mim-1 protein (myb-induced myeloid protein-1) [2].
• Purification and primary amino acid sequence of a novel neutrophil chemotactic factor LECT2 [3].
• Auto-ADP-ribosylated transferase showed higher activity than did the unmodified transferase in catalyzing ADP-ribosylation of the basic acceptor such as poly(L-arginine) and p33 while to ADP-ribosylate the acidic proteins such as casein, the modified transferase was less active [4].
• The automodified transferase was not chased by a large excess of nonradioactive NAD and did not catalyze transfer of its ADP-ribose to p33, an endogenous substrate protein for the transferase in heterophils, therefore, that automodified transferase cannot serve as an intermediate in ADP-ribosylation of other proteins [4].
• [32P]ADP-ribosylation of p33 occurred in the extracellular space, induced by the stimulus of A23187 or opsonized zymosan in the presence of [32P]NAD [5].

Biological context of LECT2

• The primary amino acid sequence revealed that the chemotactic factor was significantly different from other known chemotactic factors, indicating a novel protein designated LECT2 [3].
• Exocytosis of arginine-specific ADP-ribosyltransferase and p33 induced by A23187 and calcium or serum-opsonized zymosan in chicken polymorphonuclear leukocytes [5].

Anatomical context of LECT2

• In addition to actin, caldesmon and tropomyosin, p33 was contained in the native thin filaments prepared from smooth muscle [6].
• An actin-binding protein (p33) has been purified from chicken gizzard smooth muscle [6].
• We earlier reported the co-localization of arginine-specific ADP-ribosyltransferase [EC 2.4.2.31] and its target protein p33 (mim-1 protein) in cytoplasmic granules in chicken polymorphonuclear leukocytes (so-called heterophils) [Mishima, K., Terashima, M., Obara, S., Yamada, K., Imai, K., and Shimoyama, M. (1991) J. Biochem. 110, 388-394] [5].

Analytical, diagnostic and therapeutic context of LECT2

• Molecular cloning of human and bovine LECT2 having a neutrophil chemotactic activity and its specific expression in the liver [1].
• Percoll density gradient centrifugation of the postnuclear fraction of the heterophils revealed the co-localization of ADP-ribosyltransferase with p33 in the granule fraction [7].

References