Cytoplasmic tail. The extracellular component of GPNMB is composed of an RGD motif that binds to integrin, preserving cell ell adhesion, and an Ig-like polycystic kidney illness domain involved in protein rotein and protein arbohydrate interactions [11]. The extracellular fragment of GPNMB is cleaved by ADAM10 around the plasma membrane and secreted into the extracellular space [9,13]. GPNMB is important for the invasion and metastasis of many cancers [11] and plays diverse roles in typical cells, like T-cell inactivation [14] as well as the promotion with the specialization of osteoclasts and osteoblasts [15,16]. Additionally, higher GPNMB protein levels had been observed in the cerebrospinal fluid, serum, and spinal cord of patients with amyotrophic lateral sclerosis [17]. Other studies have shown that the soluble type of GPNMB (sGPNMB) mediates signal transduction via cell surface proteins, like CD44, as receptors for sGPNMB, showing anti-inflammatory or neuroprotective Pantoprazole-d6 MedChemExpress effects [18,19]. Within the skin epidermis, GPNMB has been reported to be mainly expressed in melanocytes and regulated by microphthalmia-associated transcription aspect (MITF), playing a crucial role in pigmentation [20]. In melanocytes, GPNMB shares significant amino acid sequence homology with all the melanosome protein Pmel-17 (25 amino acid sequence homology); It’s present in all stages (I V) of melanosomes and is crucial for the formation of melanosomes [10,21]. GPNMB functions as an adhesion protein amongst melanocytes and keratinocytes via integrin [22]. Until lately, the expression and function of GPNMB in