Disease relevance of CALML5

• No degradation of CLSP in psoriatic epidermis keeping its ability to bind protein as transglutaminase 3 may have a physiological role in skin diseases such as psoriasis [1].

High impact information on CALML5

• Sequencing of a rCLSP affinity purified protein revealed 100% identity with transglutaminase 3, a key enzyme in terminal differentiation, indicating an important role of CLSP in this process [2].
• We named this new protein calmodulin-like skin protein (CLSP), since reverse transcriptase-polymerase chain reaction studies of CLSP expression in 10 different human tissues revealed that this protein was particularly abundant in the epidermis where its expression is directly related to keratinocyte differentiation [2].
• In the complex, CLSP binds Ca(2+) with high affinity to all four binding sites [3].
• Thus, as fast skeletal muscle troponin C (TnC), CLSP possesses two high-affinity Ca(2+)-Mg(2+) mixed sites and two low-affinity Ca(2+)-specific sites [3].
• The Ca(2+)-dependency of the two conformational changes is biphasic in the absence of Mg(2+), but monophasic in the presence of 2 mM Mg(2+), both corresponding closely to direct binding of Ca(2+) to CLSP [3].

Biological context of CALML5

• Human CLSP, a new Ca(2+)-binding protein specifically expressed in differentiated keratinocytes, is a 15.9 kDa, four EF-hand containing protein with 52% sequence identity to calmodulin (CaM) [3].
• The expression of the calmodulin-like skin protein, a recently discovered new skin-specific calcium binding protein, was studied in cultured keratinocytes, reconstructed human epidermis, and normal human skin [4].
• Using a calmodulin-like skin protein specific polyclonal antibody and Western blot analysis we could show that in cultured keratinocytes calmodulin-like skin protein expression is strongly induced after stimulating cell differentiation by increasing the medium calcium concentration [4].

Associations of CALML5 with chemical compounds

• In the presence of Ca(2+), human CLSP forms a high-affinity 1:1 complex with melittin, a natural peptide considered to be a model for the interaction of CaM with its targets [3].
• A more than 10-fold increase was observed in the presence of sodium butyrate, whereas CD 367 abolished almost completely calmodulin-like skin protein expression already at nanomolar concentrations [4].
• In general, after 20 min CMCR solution exposure, the AFM topographical parameters were reduced for Vita Omega, and increased for Vita Alpha", whereas the CLSP topographical parameters of Procera AllTitan were slightly reduced [5].

Other interactions of CALML5

• Among the mRNAs with altered steady-state(1) levels in sun-damaged skin, we detected those encoding keratin 1, macrophage inhibitory factor, and calmodulin-like skin protein [6].

References