Sequential release of both basic and acidic isoperoxidases to the media of suspension cultured cells of Capsicum annuum

Cuenca, José; García-Florenciano, E.; Barceló, A. Ros; Muñoz, Romualdo

doi:10.1007/bf00269051

Cited by 9 publications

(7 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As was the case for the grapevine peroxidase isoenzyme group BPrx Hpl, lupin peroxidase isoenzyme group BPrx Hpl was recovered with a yield of 93% in the vacuole fraction (Table II). Similar results (Table II) were found in Capsicum annuum (7,8), lettuce (Lactuca sativa) (9) and catharanthus (Catharanthus roseus) (10).…”

Section: The Bprx Hpl Isoenzyme Group: a Distinctive Peroxidase Isoensupporting

confidence: 89%

Specific Compartmentalization of Peroxidase Isoenzymes in Relation to Lignin Biosynthesis in the Plant Cell

Barceló

Morales

Pedreño

1998

ACS Symposium Series

View full text Add to dashboard Cite

The compartmentalization of peroxidase isoenzymes related to lignin biosynthesis was studied in the cell walls and the cell wall-free spaces of several woody and non-woody plant species. The results illustrate a specific compartmentalization of peroxidase isoenzymes in cell walls compared with that found in vacuoles. Cell wall peroxidase isoenzymes may be classified into three main groups: one with acidic pI (APrx), and two with a basic pI (BPrx LpI and BPrx HpI). While basic peroxidases are constitutively expressed, acidic peroxidases are normally developmentally regulated. This developmental regulation and the greater efficacy in the oxidation of coniferyl alcohol shown by acidic peroxidases suggest that this isoenzyme group plays a key role in lignin biosynthesis, although some contribution to this process by basic peroxidases cannot be ruled out.Peroxidase (EC 1.11.1.7) is the enzyme responsible for the linking and cross-linking of monolignols during the biosynthesis of lignins in the plant cell wall. As may be expected from its specific role in lignin biosynthesis, peroxidase is mainly located in the cell wall, although other subcellular localizations have been reported. Over the last few years, considerable information has been accumulated about the subcellular localization of peroxidase isoenzymes (7). However, it remains unclear whether the findings concerning isoenzyme localization in a few plants can be generalized and rationalized. Combined histochemical, cytochemical and biochemical studies are necessary to rationalize some concepts which are only just beginning to be understood.To cast light on this question, we have studied peroxidase isoenzyme localization in lupin (Lupinus albus) (2-4), grapevine (Vitis vinifera) (5, 6), pepper (Capsicum annuum) (7, 8), lettuce (Lactuca sativa) (9), catharanthus (Catharanthus roseus) (10), oats (Avena sativa) (Rojas, M.C.; Ros Barcelo, A., unpublished data) and aleppo pine (Pinus halepensis) (Ros Barcelo, A., unpublished data). Electron microscope cytochemistry, vacuum infiltration and subcellular fractionation, together with protoplast and vacuole isolation techniques, show that in all the studied plant materials both basic (BPrx, pi > 7.0) and acidic (APrx, pi < 7.0) peroxidase isoenzymes are located in the cell wall free spaces, probably in equilibrium with those bound to the cell 84

show abstract

Section: The Bprx Hpl Isoenzyme Group: a Distinctive Peroxidase Isoensupporting

confidence: 89%

Specific Compartmentalization of Peroxidase Isoenzymes in Relation to Lignin Biosynthesis in the Plant Cell

Barceló

Morales

Pedreño

1998

ACS Symposium Series

View full text Add to dashboard Cite

show abstract

“…2). A similar variation in the level of extracellular peroxidase activity has been found for suspension cell cultures of Capsicum annuum (Cuenca et al 1989) and Gamay grapevine cultures (Garcia-Florenciano et al 1991).…”

Section: Resultssupporting

confidence: 71%

Constitutive expression of extracellular peroxidase isoenzymes capable of oxidizing 4-hydroxystilbenes during the growth cycle of grapevine suspension cell cultures

Calderón¹,

Zapata²,

Pedreño³

et al. 1994

Biol. plant.

View full text Add to dashboard Cite

The constitutive expression of peroxidase isoenzymes which are capable of oxidizing 4-hydroxystilbenes was studied during the growth cycle of suspension cell cultures from grapevine (Vitis vinifera L. cv. Monastrell) berries. The results showed that the growth of suspension cell cultures is accompanied by the constitutive expression of the peroxidase isoenzymes HSPrx 1 and HSPrx 2, previously characterised by their properties for oxidizing 4-hydroxystilbene, the expression of these isoenzymes being characteristic of Monastrell vines brought to a resistant state. However, although the differential catalytic properties of these grapevine isoenzymes are also shown by the horseradish peroxidase, no immunological relationships have been found between the peroxidases from either source.

show abstract

“…In at least four species under different treatments, we have established correlations between growth limitation, lignin accumulation, and increase of total peroxidase activity and ethylene emission (Table 1). It was found that during growth responses to several stimuli, peroxidase varied in a two-step manner, with an early variation of cationic (basic) isoperoxidases preceding changes in anionic (acidic) ones (Boyer et al, 1983;Gaspar et al, 1985a;Cuenca et al, 1989). Because there were arguments to involve basic and acidic peroxidases in auxin catabolism, in ethylene production, and in lignin polymerization, respectively, a general scheme involving sequential events, including changes in IAA level, ethylene production, and growth limitation through lignin-induced wall rigidification, was drawn ( Fig.…”

Section: Sequential Intervention Of Different Hormones In Growth Procmentioning

confidence: 99%

Changing concepts in plant hormone action

Gaspar

Kevers

Faivre‐Rampant

et al. 2003

In Vitro Cell. Dev. Biol. - Plant

View full text Add to dashboard Cite

A plant hormone is not, in the classic animal sense, a chemical synthesized in one organ, transported to a second organ to exert a chemical action to control a physiological event. Any phytohormone can be synthesized everywhere and can influence different growth and development processes at different places. The concept of physiological activity under hormonal control cannot be dissociated from changes in concentrations at the site of action, from spatial differences and changes in the tissue's sensitivity to the compound, from its transport and its metabolism, from balances and interactions with the other phytohormones, or in their metabolic relationships, and in their signaling pathways as well. Secondary messengers are also involved. Hormonal involvement in physiological processes can appear through several distinct manifestations (as environmental sensors, homeostatic regulators and spatio-temporal synchronizers, resource allocators, biotime adjusters, etc.), dependent on or integrated with the primary biochemical pathways. The time has also passed for the hypothesized ‘specific' developmental hormones, rhizocaline, canlocaline, and florigen: root, stem, and flower formation result from a sequential control of specific events at the right places through a coordinated control by electrical signals, the known phytohormones and nonspecific molecules of primary and secondary metabolism, and involve both cytoplasmic and apoplastic compartments. These contemporary views are examined in this review

show abstract

Sequential release of both basic and acidic isoperoxidases to the media of suspension cultured cells of Capsicum annuum

Cited by 9 publications

References 17 publications

Specific Compartmentalization of Peroxidase Isoenzymes in Relation to Lignin Biosynthesis in the Plant Cell

Specific Compartmentalization of Peroxidase Isoenzymes in Relation to Lignin Biosynthesis in the Plant Cell

Constitutive expression of extracellular peroxidase isoenzymes capable of oxidizing 4-hydroxystilbenes during the growth cycle of grapevine suspension cell cultures

Changing concepts in plant hormone action

Contact Info

Product

Resources

About