The multifunctional family of secreted proteins containing a C-type lectin-like domain linked to a short N-terminal peptide

• Published in: Biochimica et biophysica acta Vol. 1723; no. 1; pp. 8 - 18
• Main Authors: Iovanna, Juan L., Dagorn, Jean-Charles
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 25.05.2005
• Subjects: Amino Acid Sequence; Animals; C-type lectin; Calcium-Binding Proteins - analysis; Calcium-Binding Proteins - chemistry; Calcium-Binding Proteins - physiology; CTLD; Humans; Lithostathine; Molecular Sequence Data; Nerve Tissue Proteins - analysis; Nerve Tissue Proteins - chemistry; Nerve Tissue Proteins - physiology; PAP/p23/xHIP; PSP/Lithostathine/reg/PTP; Reg1 like; RegIV; Signal Transduction; Similar to PAP; PSP/Lithostathine/reg/PTP; IL22; CNTF; TNFα; HMG-I/Y; PAP/p23/xHIP; ADP; MPO; PTP; LPS; RegIV; RT-PCR; PPARPγ; Reg1L; C-type lectin; IFNγ; IL10; CTLD-LSNP; Similar to PAP; NFκB; STAT1; PKA; STAT3; PI3-kinase; PSP; TNBS; Reg1 like; HIP; IL1; MAPK ERK1/2; IL6; RegI; IL10Rβ; CTLD; GRF; MEK1; PAP
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2005.01.002

PSP/Lithostathine/PTP/regI, PAP/p23/HIP, reg1L, regIV and “similar to PAP” are the members of a multifunctional family of secreted proteins containing a C-type lectin-like domain linked to a short N-terminal peptide. The expression of this group of proteins is controlled by complex mechanisms, some members being constitutively expressed in certain tissues while, in others, they require activation by several factors. These members have several apparently unrelated biological effects, depending on the member studied and the target cell. These proteins may act as mitogenic, antiapoptotic or anti-inflammatory factors, can regulate cellular adhesion, promote bacterial aggregation, inhibit CaCO 3 crystal growth or increase resistance to antitumoral agents. The presence of specific receptors for these proteins is suggested because biological effects were observed after the addition of purified protein to culture media or after systemic administration to animals, whereas other biological effects could be explained by their biochemical capacity to form homo or heteromers or to form insoluble fibrils at physiological pH.