Rapid appearance of β-amyloid precursor protein immunoreactivity in damaged axons and reactive glial cells in rat brain following needle stab injury

Otsuka, Naruhito; Tomonaga, Masanori; Ikeda, Kazuhiko

doi:10.1016/0006-8993(91)91422-w

Cited by 147 publications

(73 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Further, the overexpression of APP suggests the possibility of an Alzheimer disease-like pathology after traumatic brain injury (Rumble et al, 1989). Previously, the appearance of APP in the brain during pathological events was usually attributed to its synthesis by neurons, macrophages, microglia or astrocytes (Otsuka et al, 1991). However, APP was synthesized by neurons, as showing by immunohistochemical, ELISA and RT-PCR obtained performed in this study.…”

Section: Discussionsupporting

confidence: 53%

“…Some reports have shown that the expression of APP is enhanced by various forms of brain injury, including traumatic (Otsuka et al, 1991), chemical (Nakamura et al, 1992) , and ischemic injury (Stephenson et al, 1992). Further, the overexpression of APP suggests the possibility of an Alzheimer disease-like pathology after traumatic brain injury (Rumble et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

“…Following the initial mechanical insult, secondary pathways are activated that contribute to the ischemic damage induced by circulatory disturbance, blood-brain barrier disruption and excitotoxic damage (Kawamata et al, 1995;Azbill et al, 1997;Xiong et al, 1997). The expression of APP has also been shown to increase in swollen axons and neuronal perikarya after neuronal injuries, including ischemia (Stephenson et al, 1992) and stab injuries (Otsuka et al, 1991). CNS disorders can be caused by the widespread neuronal and axonal degeneration induced by TBI (Chirumamilla et al, 2002;Rice et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, the overexpression of APP is an important factor in the neuronal degeneration of AD (Murakami et al, 1998). The expression of APP has also been shown to increase in swollen axons and neuronal perikarya after neuronal injury, including ischemia (Stephenson et al, 1992) and stab injury (Otsuka et al, 1991). As the pathological findings in dementia pugilistica mimic those in AD (Roberts et al, 1990), it has been posited that traumatic brain injury (TBI) is an epidemiological risk factor for AD (Schofield et al, 1997;DeKosky et al, 2007), although other genetic factors, which include the apoE genotype, might act additively (Nicoll et al, 1995;DeKosky et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Expression and Cerebral Function of Amyloid Precursor Protein After Rat Traumatic Brain Injury

Itoh¹,

Imano²,

Nishida³

et al. 2011

Alzheimer's Disease Pathogenesis-Core Concepts, Shifting Paradigms and Therapeutic Targets

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 53%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Expression and Cerebral Function of Amyloid Precursor Protein After Rat Traumatic Brain Injury

Itoh¹,

Imano²,

Nishida³

et al. 2011

Alzheimer's Disease Pathogenesis-Core Concepts, Shifting Paradigms and Therapeutic Targets

View full text Add to dashboard Cite

“…The axonal damage, which was evaluated after one (median 163.3 APP + axons/mm 2 ) or three (median 129.2 APP + axons/mm 2 ) weeks of remyelination in the present work, was much higher than the axonal damage observed in the study of Manrique‐Hoyos and colleagues, indicating that axonal damage is more prevalent early after cuprizone‐diet cessation. Furthermore, damaged or transected axons could be detected by immunohistochemistry for APP already a few hours after injury (McKenzie et al, 1996; Otsuka, Tomonaga, & Ikeda, 1991) and were observed up to four weeks after the insult (Bramlett, Kraydieh, Green, & Dietrich, 1997; Pierce, Trojanowski, Graham, Smith, & McIntosh, 1996). Therefore, the majority of the axonal damage probably occurred during cuprizone treatment and demyelination and was still detectable during the phase of remyelination.…”

Section: Discussionmentioning

confidence: 99%

Acutely damaged axons are remyelinated in multiple sclerosis and experimental models of demyelination

Schultz

Meer

Wrzos

et al. 2017

Glia

View full text Add to dashboard Cite

Remyelination is in the center of new therapies for the treatment of multiple sclerosis to resolve and improve disease symptoms and protect axons from further damage. Although remyelination is considered beneficial in the long term, it is not known, whether this is also the case early in lesion formation. Additionally, the precise timing of acute axonal damage and remyelination has not been assessed so far. To shed light onto the interrelation between axons and the myelin sheath during de‐ and remyelination, we employed cuprizone‐ and focal lysolecithin‐induced demyelination and performed time course experiments assessing the evolution of early and late stage remyelination and axonal damage. We observed damaged axons with signs of remyelination after cuprizone diet cessation and lysolecithin injection. Similar observations were made in early multiple sclerosis lesions. To assess the correlation of remyelination and axonal damage in multiple sclerosis lesions, we took advantage of a cohort of patients with early and late stage remyelinated lesions and assessed the number of APP‐ and SMI32‐ positive damaged axons and the density of SMI31‐positive and silver impregnated preserved axons. Early de‐ and remyelinating lesions did not differ with respect to axonal density and axonal damage, but we observed a lower axonal density in late stage demyelinated multiple sclerosis lesions than in remyelinated multiple sclerosis lesions. Our findings suggest that remyelination may not only be protective over a long period of time, but may play an important role in the immediate axonal recuperation after a demyelinating insult.

show abstract

Mab22C11 antibody to amyloid precursor protein recognizes a protein associated with specific astroglial cells of the rat central nervous system characterized by their capacity to support axonal outgrowth

et al. 1997

View full text Add to dashboard Cite

Amyloid precursor protein (APP) is a transmembrane glycoprotein which is believed to promote neural cell adhesion, neural survival, and neuritogenesis. The present study was undertaken to determine whether APP could be detected within different types of astroglial cells present in the central nervous system (CNS) of neonatal or adult rats. The localization of this protein within glial cells was studied by using a monoclonal antibody (Mab22C11) that recognizes all APP isoforms and in addition cross-reacts with APP-like proteins. In the brain of neonatal rats, Mab22C11 immunostaining was associated with numerous elongated radial glia-like structures. In the intact brain and spinal cord of adult rats, Mab22C11 immunostaining was associated with (i) numerous neuron-like structures and (ii) glial structures immunostained for glial fibrillary acidic protein (GFAP) and/or vimentin, including tanycytes mostly located in the mediobasal hypothalamus, fibrous astrocytes located in the white matter and ependymocytes bordering the ventricles. On the other hand, all the GFAP-immunostained astrocytes located in the grey matter were Mab22C11 negative. In the lesioned brain and spinal cord of adult rats, Mab22C11 immunostaining was associated with intensely GFAP-immunostained reactive astrocytes located close to a surgical lesion, but not with those induced by Wallerian degeneration that appear at a distance from a lesion. Electron microscopic observations further indicated that in all these labeled astroglial cells, Mab22C11 immunostaining was mainly localized to the limiting plasma membrane and the membrane of intracytoplasmic cisternae and vesicles. These data indicate that Mab22C11 antibody induces strong immunostaining of specific astroglial cells of the neonatal and adult rat CNS that support axonal outgrowth, therefore suggesting that an APP-like protein associated with these cells participates in their axonal outgrowth promoting properties.

show abstract

Rapid appearance of β-amyloid precursor protein immunoreactivity in damaged axons and reactive glial cells in rat brain following needle stab injury

Cited by 147 publications

References 13 publications

Expression and Cerebral Function of Amyloid Precursor Protein After Rat Traumatic Brain Injury

Expression and Cerebral Function of Amyloid Precursor Protein After Rat Traumatic Brain Injury

Acutely damaged axons are remyelinated in multiple sclerosis and experimental models of demyelination

Mab22C11 antibody to amyloid precursor protein recognizes a protein associated with specific astroglial cells of the rat central nervous system characterized by their capacity to support axonal outgrowth

Contact Info

Product

Resources

About