Pérez-Ibave Diana Cristina, González-Alvarez Rafael, de La Luz Martinez-Fierro Margarita, Ruiz-Ayma Gabriel, Luna-Muñoz Maricela, Martínez-De-Villarreal Laura Elia, De Lourdes Garza-Rodríguez María, Reséndez-Pérez Diana, Mohamed-Noriega Jibran, Garza-Guajardo Raquel, Bautista-De-Lucío Víctor Manuel, Mohamed-Noriega Karim, Barboza-Quintana Oralia, Arámburo-De-La-Hoz Carlos, Barrera-Saldaña Hugo Alberto, Rodríguez-Sánchez Irám Pablo
Servicio de Oncología, Universidad Autónoma de Nuevo León, Hospital Universitario "Dr. José Eleuterio González", Monterrey, Nuevo León, Mexico.
Facultad de Medicina, Universidad Autónoma de Guadalajara, Zapopan, Jalisco, Mexico.
Biol Res. 2016 Nov 8;49(1):44. doi: 10.1186/s40659-016-0101-8.
The olfactomedin-like domain (OLFML) is present in at least four families of proteins, including OLFML2A and OLFML2B, which are expressed in adult rat retina cells. However, no expression of their orthologous has ever been reported in human and baboon.
The aim of this study was to investigate the expression of OLFML2A and OLFML2B in ocular tissues of baboons (Papio hamadryas) and humans, as a key to elucidate OLFML function in eye physiology.
OLFML2A and OLFML2B cDNA detection in ocular tissues of these species was performed by RT-PCR. The amplicons were cloned and sequenced, phylogenetically analyzed and their proteins products were confirmed by immunofluorescence assays.
OLFML2A and OLFML2B transcripts were found in human cornea, lens and retina and in baboon cornea, lens, iris and retina. The baboon OLFML2A and OLFML2B ORF sequences have 96% similarity with their human's orthologous. OLFML2A and OLFML2B evolution fits the hypothesis of purifying selection. Phylogenetic analysis shows clear orthology in OLFML2A genes, while OLFML2B orthology is not clear.
Expression of OLFML2A and OLFML2B in human and baboon ocular tissues, including their high similarity, make the baboon a powerful model to deduce the physiological and/or metabolic function of these proteins in the eye.
嗅觉介质样结构域(OLFML)存在于至少四个蛋白质家族中,包括OLFML2A和OLFML2B,它们在成年大鼠视网膜细胞中表达。然而,从未有人报道过它们在人类和狒狒中的直系同源物的表达情况。
本研究旨在调查OLFML2A和OLFML2B在狒狒(阿拉伯狒狒)和人类眼组织中的表达情况,作为阐明OLFML在眼生理学中功能的关键。
通过逆转录聚合酶链反应(RT-PCR)检测这些物种眼组织中的OLFML2A和OLFML2B cDNA。对扩增产物进行克隆和测序,进行系统发育分析,并通过免疫荧光测定法确认其蛋白质产物。
在人角膜、晶状体和视网膜以及狒狒角膜、晶状体、虹膜和视网膜中发现了OLFML2A和OLFML2B转录本。狒狒的OLFML2A和OLFML2B开放阅读框序列与其人类直系同源物具有96%的相似性。OLFML2A和OLFML2B的进化符合纯化选择的假设。系统发育分析显示OLFML2A基因存在明显的直系同源关系,而OLFML2B的直系同源关系不明确。
OLFML2A和OLFML2B在人类和狒狒眼组织中的表达,包括它们的高度相似性,使狒狒成为推断这些蛋白质在眼中生理和/或代谢功能的有力模型。