Changes of calretinin, calbindin D28K and parvalbumin-immunoreactive neurons in the superficial layers of the hamster superior colliculus following monocular enucleation

Neurosci Lett. 2002 Sep 13;330(1):104-8. doi: 10.1016/s0304-3940(02)00723-1.

Abstract

We studied the effects of monocular enucleation on the patterned distribution of calretinin-, calbindin D28K- and parvalbumin-immunoreactive (IR) neurons in the superficial layers of the hamster superior colliculus (SC). The calcium-binding proteins were localized using antibody immunocytochemistry. Almost complete depletion of the calretinin-IR fibers in the superficial layers of the contralateral SC was found following unilateral enucleation. Quantitative analysis showed that on the experimental side of the SC, an enormous number of calretinin-IR cells newly appeared (716%). On the experimental side of the SC, the number of parvalbumin-IR cells also increased (32%). By contrast, on the experimental side of the SC, the number of calbindin D28K-IR cells exhibited a reduction (43%). Two-color immunofluorescence revealed that none of the newly appeared calretinin-IR cells were labeled with antibodies to calbindin D28K or parvalbumin. The present results demonstrate that retinal projection may control the activity of the expression of these calcium-binding proteins in the hamster SC but in different manners. The results also show that the patterned change of calretinin and parvalbumin in the hamster SC is comparable with other animals, but the change of calbindin D28K is not identical.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calbindin 2
  • Calbindins
  • Cricetinae
  • Eye Enucleation*
  • Neural Pathways / chemistry
  • Neural Pathways / metabolism
  • Neurons / chemistry
  • Neurons / metabolism*
  • Parvalbumins / analysis
  • Parvalbumins / metabolism*
  • S100 Calcium Binding Protein G / analysis
  • S100 Calcium Binding Protein G / metabolism*
  • Superior Colliculi / chemistry
  • Superior Colliculi / metabolism*

Substances

  • Calbindin 2
  • Calbindins
  • Parvalbumins
  • S100 Calcium Binding Protein G