title: A comparative study of the calcium-binding proteins calbindin-D28K, calretinin, calmodulin and parvalbumin in the rat spinal cord.
abstract: Comparison of the immunocytochemical localizations revealed distinct patterns of differential distribution and overlapping of calbindin-D28K (CB-D28K), calretinin (CR), calmodulin (CM) and parvalbumin (PV) in the rat spinal cord. In some areas, one of the four calcium-binding proteins (CBPs) appears to be predominant, for example, CB-D28K in lamina I and ependymal cells, PV at the inner part of laminae II, CR in laminae V and VI and CM in motoneurons of lamina IX. In other regions of the spinal cord, more than one CBPs was abundant. CB-D28K and CR were similarly distributed in lamina II and the lateral spinal and cervical nucleus; CM and PV were similarly abundant in the ventromedial dorsal horn, internal basilar and central cervical nucleus; CR and PV were similarly abundant in the ventromedial dorsal horn, internal basilar and central cervical nucleus; CR and PV were similarly heterogeneous in the gracile fasciculus from caudal to rostral spinal cord. In the sacral dorsal gray commissure, the distribution patterns of CR and PV were clearly complementary. The unilateral ganglionectomies resulted in a substantial reduction of CBP-like immunoreactivity (CBP-LI) in the dorsal columns and a reduction of CM- and PV-LI in the ventromedial dorsal horn. In the motor system, only CM labeled large motoneurons in lamina IX and CB-D28K lightly stained pyramidal tract. The apparent absence of CM-LI in the superficial dorsal horn is contradictory to the presence of a CM-dependent nitric oxide synthase in the region. These data indicate that most CBP-LI in the dorsal column pathway had primary afferent origin, while the superficial dorsal horn exhibited intrinsic CBP immunoreactivity. The differential and selective localizations of CBPs in the spinal cord suggest a role for these proteins in spinal nociceptive processing, visceral regulation and dorsal column sensory pathways.
authors.affiliation: Neurobiology and Anesthesiology Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892.
authors.forename: K
authors.initials: K
authors.lastname: Ren
authors.forename: M A
authors.initials: MA
authors.lastname: Ruda
mesh_terms: D000818:Animals; D064092:Calbindin 1; D064032:Calbindin 2; D064026:Calbindins; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D002147:Calmodulin / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D006801:Humans; D010320:Parvalbumins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D051381:Rats; D064030:S100 Calcium Binding Protein G / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D013116:Spinal Cord / Q000033:anatomy & histology / Q000737:chemistry / Q000378:metabolism*
chemical_list: C576498:CALB1 protein, human; C576764:CALB2 protein, human; C576500:Calb1 protein, rat; C576512:Calb2 protein, rat; D064092:Calbindin 1; D064032:Calbindin 2; D064026:Calbindins; D002135:Calcium-Binding Proteins; D002147:Calmodulin; D010320:Parvalbumins; D064030:S100 Calcium Binding Protein G